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|Mutation Type||critical splice donor site (2 bp from exon)|
|Coordinate||60,520,914 bp (GRCm38)|
|Base Change||T ⇒ C (forward strand)|
|Gene Name||myosin XV|
|Synonym(s)||sh2; sh-2; Myo15a|
|Chromosomal Location||60,469,339-60,528,369 bp (+)|
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes an unconventional myosin. This protein differs from other myosins in that it has a long N-terminal extension preceding the conserved motor domain. Studies in mice suggest that this protein is necessary for actin organization in the hair cells of the cochlea. Mutations in this gene have been associated with profound, congenital, neurosensory, nonsyndromal deafness. This gene is located within the Smith-Magenis syndrome region on chromosome 17. Read-through transcripts containing an upstream gene and this gene have been identified, but they are not thought to encode a fusion protein. Several alternatively spliced transcript variants have been described, but their full length sequences have not been determined. [provided by RefSeq, Jul 2008]
PHENOTYPE: Mutations in this gene result in profound deafness and neurological behavior. [provided by MGI curators]
|Amino Acid Change|
|Institutional Source||Beutler Lab|
|Gene Model||predicted gene model for protein(s): [ENSMUSP00000071777] [ENSMUSP00000080507] [ENSMUSP00000091686]|
|Predicted Effect||probably null|
|Predicted Effect||probably null|
|Predicted Effect||probably null|
|Alleles Listed at MGI|
|Mode of Inheritance||Autosomal Recessive|
|Local Stock||Live Mice|
|Last Updated||2017-03-02 9:36 AM by Katherine Timer|
|Record Created||2013-07-01 9:29 AM by Jennifer Weatherly|
The parker phenotype was initially identified among G3 mice of the pedigree R0477, some of which displayed constant movement of the head from side-to-side, head tilt, circling behavior, and wobbling (Figure 1).
|Nature of Mutation|
Whole exome HiSeq sequencing of the G1 grandsire identified 56 mutations. The vesitbular phenotype was linked to a mutation in Myo15: a T to C transition at 60,520,914 on chromosome 11, corresponding to base pair 51,576 in GenBank genomic region NC_000077. Linkage was found with a recessive model of inheritance (P = 4.307 x 10-5), wherein 6 variant homozygotes departed phenotypically from 46 unaffected mice that were either homozygous variant (n = 9), heterozygous (n = 19), or homozygous for the reference allele (n = 18) (Figure 2). Myo15 encodes several isoforms including a long isoform (NM_182698; isoform 1; contains 66 total exons) and two others that lack in-frame exons in the 5’ coding region (isoform 2a (NM_182698; contains 64 total exons) and isoform 3 (NM_001103171; contains 65 total exons); see “Protein Prediction" for more details. The mutation is located in the donor splice site of intron 61 in isoform 1, intron 59 in isoform 2a, and intron 60 in isoform 3, two nucleotides from the previous exon in each transcript. The effect of the mutation at the cDNA and protein level of each isoform is unknown. One possibility, shown below, is that aberrant splicing may result in the skipping of the 161 base pair preceding exon (exon 61 in isoform 1 (shown); alternatively, exon 59 in isoform 2a and exon 60 in isoform 3) and splicing from exon 60 to exon 62 in isoform 1 (alternatively, splicing from exon 58 to exon 60 in isoform 2a or splicing from exon 59 to exon 61 in isoform 3). The aberrant splicing would lead to a deletion of 53 amino acids (amino acids 3244-3297) as well as a frameshift and subsequent coding of a premature stop codon.
<--exon 60 <--exon 61--> intron 61--> exon 62-->
49134 ……GTCACCAACCGAG GCCAGCACGTGTGT……ATGCACTACAATCAG gtcagagatg………GTTCTGCCTGA
3240 ……-V--T--N--R-- G--Q--H--V--C-……-M--H--Y--N--Q- G--S--A--*
correct deleted aberrant
Genomic numbering corresponds to NC_000077. Isoform 1 is shown. The donor splice site of intron 61 of Myo15, which is destroyed by the mutation, is indicated in blue; the mutated nucleotide is indicated in red.
Myosins are divided into conventional (muscle myosins and myosins similar in structure and function to muscle myosins, all belonging to class II) and unconventional classes (myosins that do not resemble muscle myosins). Myo15 encodes myosin XV (alternatively, Myosin XVa), a 3,511 amino acid member of the unconventional myosin family.
Myosin XV has a proline-rich N-terminal extension [Figure 3; amino acids 1-1200; SMART; (2;3)]. The N-terminal extension is encoded by exon 2 does not have sequence similarity to reported proteins and the function is unknown (2;4). Mouse Myo15 encodes transcript variants: isoform 1 encodes the full-length class 1 myosin XV protein, isoform 2a encodes a myosin XV protein without exon 2 and exon 26, and isoform 3 encodes a myosin XV protein without exon 2; all three isoforms are functional. Analysis of inner ear human MYO15 cDNAs determined that there are also several alternatively spliced MYO15 transcripts in human (3). The MYO15 cDNAs were individually missing exons 2, 8, 26, 30, 40, and 61 (3). Skipping of exons 30, 40, or 61 resulted in a frameshift that terminated the open reading frame shortly downstream of the missing exon (3). Skipping of exons 2, 8, or 26 did not interrupt the MYO15 reading frame (3). Exon 2 encodes the myosin XV start codon and encodes most of the 1223 amino acid N-terminal extension (3). The first start codon in-frame in the transcripts without exon 2 is located at the beginning of exon 3, coding 20 amino acids preceding the motor domain (3). Exon 8 encodes two amino acids in the motor domain, while exon 26 encodes an 18-amino acid insertion in the second IQ motif; a stop codon is introduced into the open reading frame in the long form of exon 26, resulting in truncation of the myosin XV protein after the IQ motifs (3).
Myosin XV has a highly conserved motor domain (amino acids 1200-1884; NM_010862; SMART) following the N-terminal extension (3). The motor domain contains an adenosine triphosphate (ATP)- and an actin-binding site (amino acids 1299-1306 and 1776-1783, respectively; Uniprot) (5-7). The motor domain in Nina C, a myosin expressed in the photoreceptor cells of Drosophila retinas, was necessary to maintain the structure of the photoreceptor cells (2). Missense mutations within the motor domain of myosin XV (e.g., C1779Y or R1354A;G1575A; NM_010862) resulted in mislocalization of myosin XV in the bodies of transfected wild-type auditory hair cells; the mutants were unable to properly target to the tips of the stereocilia (8).
The myosin neck region contains a variable number of light-chain binding (IQ) motifs (IQxxxRGxxxRK) and is linked to the motor domain by a converter region [(9); reviewed in (10;11)]. Myosin XV has two IQ motifs (1909-1920; LQRCLRGFFIKR and 1932-1943; LQSRARGYLARQ) (2;3;6). The IQ motif is an α-helical structure that often mediates the binding of myosins to calmodulin, members of the EF-hand family of calcium-binding proteins, or myosin light chains [reviewed in (10;11)].
The tail regions of the myosins are divergent in length and sequence (6). The myosin XV tail is 1584 amino acids in length and has two myosin tail homology 4 (MyTH4) domains (amino acids 2049-2195 and 3031-3185; SMART), a band 4.1/ezrin/radixin/moesin (FERM)-like domain (amino acids 2687-2867, human myosin XVa), a Src homology 3 (SH3) domain (amino acids 2851-2933), and a FERM domain (alternatively, talin-like domain; amino acids 3188-3400) (2;3;12;13). MyTH4 domains have an unknown function, but are found in the tails of other myosins, including myosins IV, VIIA, X, and XII as well as kinesin-like motor proteins (3;12). The MyTH4 domain is proposed to function in microtubule binding as well as in actin binding to the plasma membrane (14). FERM domains are often found in membrane-associated proteins and mediate the interaction of the FERM-containing proteins with the cytoplasmic domains of integral membrane proteins and/or they function as a mediator between the cell membrane and actin cytoskeleton (12;15;16). The FERM domain of myosin XV is proposed to be involved in anchoring myosin XV to the cell membrane (2). SH3 domains function in recognizing and binding proline-rich sequences (17). SH3 domains are often found in proteins that function in synaptic vesicle endocytosis (18) and in the proper localization of proteins (19). The function of the myosin XV SH3 domain is unknown, but it is proposed to mediate an intramolecular interaction with a region in the proline-rich N-terminal extension to regulate the activity of myosin XV (3).
Myosin XV is unique among the myosins in that it has a predicted class I PDZ-ligand motif (ITLL*) at the C-terminus (8;13;20). The PDZ-ligand motif of myosin XV is required for association of myosin XV with whirlin as well as the localization of whirlin to stereocilia tips (described in “Background”, below) (8;21).
The parker mutation is predicted to result in a loss of exon 61 (isoform 1) encoding amino acids 3244-3297. In each of the isoforms, the parker mutation is predicted to result in the loss of a portion of the C-terminal FERM domain and the subsequent coding of a premature stop codon within that domain.
Myo15 is expressed as early as embryonic day (E) 13.5 in the developing mouse inner ear (2). At E15.5, Myo15 transcripts are expressed in the cristae ampularis, macula utriculi, and macula sacculi, and cochlea in the ear (2;3). At E18.5, Myo15 is restricted to the sensory epithelium of the organ of Corti in the cochlea (2;21). At postnatal day (P) 8, Myo15 is expressed in the inner hair cells and outer hair cells of the organ of Corti within the inner ear (2). In the adult mouse, Myo15 is also expressed in the brain and liver (5).
At P7 onward, myosin XV is localized to the capping region (i.e., the location of the growth and remodeling of the actin core) of the stereocilium in the inner ear hair cells, between the upper end of the actin core and apical plasma membrane (22-24). The amount of myosin XV is directly proportional to the length of the stereocilia (13;23;24). Myosin XV continuously migrates towards the plus ends of actin filaments and accumulates at the stereocilia tips (8;21).
Expression analysis of MYO15A in human tissues has been conflicting. Wang et al. determined that MYO15A is expressed in the cochlea of 18- to 22-week fetuses as well as in human fetal and adult brain, ovary, testis, kidney, and pituitary gland (6). Liang et al. determined that MYO15 was predominantly expressed in the adult pituitary gland, with less expression in the testis and ovary; low expression (compared to the expression level in the pituitary gland) was detected in the adult human brain, kidney, liver, lung, pancreas, placenta, or skeletal muscle (3). The discrepancies between the expression analysis in the Liang et al. study compared to that of Wang et al. was attributed to the design of the probe used in the Northern blot analysis (3). Additional studies determined that myosin XV mRNA and protein are expressed in all types of normal anterior pituitary cells and pituitary tumors, several cells of all endocrine tumors of the gut and pancreas, normal endocrine cells of the small bowel, gastric, adrenal medulla, paraganglionic tissue as well as in most pancreatic islet cells (25;26). Expression was variable in pituitary cells; the most intense staining was observed in the secretory granules of adrenocorticotropic hormone, prolactin, and glycoprotein hormone-producing cells (26).
Myosins are actin-based molecular motors that generate mechanical force using the energy generated from the hydrolysis of adenosine triphosphate (ATP) (3;6). Myosins function in organelle and vesicle movement, cytokinesis, phagocytosis, signal transduction, cellular movement, membrane trafficking, regulation of ion channels, and muscle contraction (5;27;28). For more information about the general functions of myosins see mayday circler (Myo6) and new gray (Myo5a).
Each hair cell in the inner ear is comprised of a bundle of up to 300 stereocilia that project from the apical cell surface (13;29); each stereocilium is filled with up to 1000 polarized and cross-linked actin filaments [Figure 4; (22)]. The stereocilia are organized in a staircase pattern and held together by extracellular lateral projections (side-links). Deflection of the hair bundle results in gating of transducer channels at the tips of the stereocilia and subsequent modulation of the cell membrane potential that converts the sound-evoked mechanical stimulus into an electrical signal (i.e., mechano-electrical transduction) (29;30). For more information about proteins involved in the maintenance and function of the hair cells of the inner ear please see the records for dee dee and squirm. Myosin XI (see mayday circler) also functions in the development and/or maintenance of sensory hair cells; the function of myosin XV and myosin XI do not overlap (9). Myosin XV functions in the assembly and maintenance of actin organization in hair cells of the inner ear by acting as a motor and carrier along the length of the actin filament within the hair cells (31). Myosin XV senses the tension between the plasma membrane and the actin filaments, a function that is necessary in the growth of the steocilia (13). Myosin XV contributes to the elongation of stereocilia by delivering whirlin, a multi-PDZ domain-containing scaffold protein, to the stereocilia tips (8). Both myosin XV and whirlin are required for the elongation and staircase formation of the stereocilia bundle and myosin XV and whirlin may function as part of a complex that modulates the growth of actin bundles in the stereocilia (8;13). Another proposed function of myosin XV is the maintenance of the hair cell mechanotransduction apparatus at the tips of the stereocilia (5;8). The function of myosin XV in endocrine cells is unknown. Within pituitary cells and pituitary adenomas, myosin XV may function in cytoplasmic organelle movement, including secretory granules and/or hormone secretion (25).
Two myosin XV mutant mouse models, shaker 2 (Myo15sh2; MGI:1857036) and shaker 2J (Myo15sh2J; MGI:1889795) have been characterized. The Myo15sh2 mutation is a tyrosine to cysteine substitution at amino acid 1779 within the myosin motor domain (5;7). The spontaneous Myo15sh2J mutation results in the deletion of the last six exons and part of the 3’ flanking region encoding the myosin XV C-terminus, including the C-terminal FERM domain (2). Both the shaker 2 and shaker 2J mice have abnormally short stereocilia bundles on the inner ear hair cells compared to wild-type mice; the bundles are correctly positioned (2;5). As a result, the shaker 2 and shaker 2J homozygous mice are congenitally deaf and exhibit vestibular defects that cause head-tossing and circling behavior (3-5). The mechanosensory activity of the short stereocilia in young shaker 2 mice are not affected despite the changes in stereocilia length (32). Further studies determined that the Myo15sh2 mutation disrupts fast adaptation and calcium sensitivity in cochlear inner hair cells (33). In the inner hair cells of young (up to P14) shaker 2 mice, the mechanosensitivity is mediated by “top-to-top” links that run perpendicular to the shortened stereocilia; the outer hair cells have a prominent staircase stereocilia arrangement and obliquely-oriented tip links (32;33). Lack of myosin XV expression allows myosin VIIa molecules to localize between the plasma membrane and actin bundle in the short stereocilia of the shaker 2 mice; no myosin XV was detected at the tips of inner ear hair cell stereocilia (22). Transfection of a green fluorescent protein (GFP)-Myo15 into shaker 2 sensory epithelial explants resulted in complete rescue of the normal length and shape of the hair bundles by 67 hours post-transfection (8). In addition, a bacterial artificial chromosome (BAC)-mediated transgene corrected the deafness and circling phenotype of shaker 2 mice and the hair cells had normal stereocilia and no unusual actin-containing structures (5). A spontaneous mutant rat model, LEW/Ztm-ci2, exhibits syndromal deafness as well as spontaneous lateralized circling behavior, locomotor hyperactivity, moderate ataxia and the inability to swim (31). The ci2 model has a leucine to proline substitution at amino acid 3157 in the myosin XV protein within the C-terminal MyTH4 domain (31). In this model, the organ of Corti was completely absent or reduced (31). The inner hair cells of the vestibular organs were present, but there was shortened stereocilia, a lower number of ganglion cells, and a reduced thickness of axons (31).
As of 2009, 24 mutations in MYO15A have been linked to autosomal recessive nonsyndromic congenital deafness [(DFNB3; OMIM: #600316); (4;6;21)]; nonsyndromic recessive deafness accounts for ~80% of hereditary hearing loss (6).
The Myo15parker mutation is predicted to be similar to the Myo15sh2J mutation; both mutations affect the C-terminal FERM domain and result in the deletion of the last six exons of Myo15 (2). Similar to the shaker 2J mice, the parker mice exhibit head-tossing and circling behavior. Anderson et al. propose that the myosin XVshaker 2J protein is unable to exert force on the actin cytoskeleton because the truncated protein is improperly anchored, resulting in a failure to form the scaffolding to form the normal stereocilia structure (2).
parker(F):5'- GCATGTGGCTTAGACCACAGTGTTC -3'
parker(R):5'- GCACACTATCAGGCTATGCAGAGG -3'
parker_seq(F):5'- AGACCACAGTGTTCCTTCTTC -3'
parker_seq(R):5'- agctggcctggagcttg -3'
Parker genotyping is performed by amplifying the region containing the mutation using PCR, followed by sequencing of the amplified region to detect the single nucleotide transition.
Parker(F): 5’- GCATGTGGCTTAGACCACAGTGTTC-3’
Parker(R): 5’- GCACACTATCAGGCTATGCAGAGG-3’
Parker_seq(F): 5’- AGACCACAGTGTTCCTTCTTC-3’
1) 94°C 2:00
2) 94°C 0:30
3) 55°C 0:30
4) 72°C 1:00
5) repeat steps (2-4) 40X
6) 72°C 10:00
7) 4°C ∞
The following sequence of 533 nucleotides from GenBank genomic region NC_000077 encoding Myo15) is amplified:
51361 gtggcttaga ccacagtgtt ccttcttcca gccgtgcctc tttctccctg caggccagca
51421 cgtgtgtcca ctgagctgcc gggcctacat actggatgtg gcctcagaga tggagcaggt
51481 ggacgggggc tacacactct ggttccggcg ggtgctttgg gatcagccac tgaagtttga
51541 gaatgagctg tatgtgacca tgcactacaa tcaggtcaga gatgcgacct ccctattgct
51601 ctgaacctac agtgccacgc ccagatgctt ggggaacttg taccaaagct ttagcaattc
51661 cacttacaaa acacaaccac gttgttggat gtggtaatgt atgccttgaa ttctagtgct
51721 caggaggcag aagcaggcag atctctgtga gttagaggcc agcctggtct acatagcaag
51781 ctccaggcca gctaaggcta tatagaaaga tcttttctga aacacacagc aacttcattc
51841 tgggaccaca tggtgttgag acctacctct gcatagcctg atagtgtgc
Primer binding sites are underlined and the sequencing primer is highlighted; the mutated nucleotide is shown in red text.
1. Suzuki, T., Li, W., Zhang, Q., Novak, E. K., Sviderskaya, E. V., Wilson, A., Bennett, D. C., Roe, B. A., Swank, R. T., and Spritz, R. A. (2001) The Gene Mutated in Cocoa Mice, Carrying a Defect of Organelle Biogenesis, is a Homologue of the Human Hermansky-Pudlak Syndrome-3 Gene. Genom. 78, 30-37.
2. Anderson, D. W., Probst, F. J., Belyantseva, I. A., Fridell, R. A., Beyer, L., Martin, D. M., Wu, D., Kachar, B., Friedman, T. B., Raphael, Y., and Camper, S. A. (2000) The Motor and Tail Regions of Myosin XV are Critical for Normal Structure and Function of Auditory and Vestibular Hair Cells. Hum Mol Genet. 9, 1729-1738.
3. Liang, Y., Wang, A., Belyantseva, I. A., Anderson, D. W., Probst, F. J., Barber, T. D., Miller, W., Touchman, J. W., Jin, L., Sullivan, S. L., Sellers, J. R., Camper, S. A., Lloyd, R. V., Kachar, B., Friedman, T. B., and Fridell, R. A. (1999) Characterization of the Human and Mouse Unconventional Myosin XV Genes Responsible for Hereditary Deafness DFNB3 and Shaker 2. Genomics. 61, 243-258.
4. Nal, N., Ahmed, Z. M., Erkal, E., Alper, O. M., Luleci, G., Dinc, O., Waryah, A. M., Ain, Q., Tasneem, S., Husnain, T., Chattaraj, P., Riazuddin, S., Boger, E., Ghosh, M., Kabra, M., Riazuddin, S., Morell, R. J., and Friedman, T. B. (2007) Mutational Spectrum of MYO15A: The Large N-Terminal Extension of Myosin XVA is Required for Hearing. Hum Mutat. 28, 1014-1019.
5. Probst, F. J., Fridell, R. A., Raphael, Y., Saunders, T. L., Wang, A., Liang, Y., Morell, R. J., Touchman, J. W., Lyons, R. H., Noben-Trauth, K., Friedman, T. B., and Camper, S. A. (1998) Correction of Deafness in Shaker-2 Mice by an Unconventional Myosin in a BAC Transgene. Science. 280, 1444-1447.
6. Wang, A., Liang, Y., Fridell, R. A., Probst, F. J., Wilcox, E. R., Touchman, J. W., Morton, C. C., Morell, R. J., Noben-Trauth, K., Camper, S. A., and Friedman, T. B. (1998) Association of Unconventional Myosin MYO15 Mutations with Human Nonsyndromic Deafness DFNB3. Science. 280, 1447-1451.
7. Cope, M. J., Whisstock, J., Rayment, I., and Kendrick-Jones, J. (1996) Conservation within the Myosin Motor Domain: Implications for Structure and Function. Structure. 4, 969-987.
8. Belyantseva, I. A., Boger, E. T., Naz, S., Frolenkov, G. I., Sellers, J. R., Ahmed, Z. M., Griffith, A. J., and Friedman, T. B. (2005) Myosin-XVa is Required for Tip Localization of Whirlin and Differential Elongation of Hair-Cell Stereocilia. Nat Cell Biol. 7, 148-156.
9. Karolyi, I. J., Probst, F. J., Beyer, L., Odeh, H., Dootz, G., Cha, K. B., Martin, D. M., Avraham, K. B., Kohrman, D., Dolan, D. F., Raphael, Y., and Camper, S. A. (2003) Myo15 Function is Distinct from Myo6, Myo7a and Pirouette Genes in Development of Cochlear Stereocilia. Hum Mol Genet. 12, 2797-2805.
10. Friedman, T. B., Sellers, J. R., and Avraham, K. B. (1999) Unconventional Myosins and the Genetics of Hearing Loss. Am J Med Genet. 89, 147-157.
11. Mooseker, M. S., and Cheney, R. E. (1995) Unconventional Myosins. Annu Rev Cell Dev Biol. 11, 633-675.
12. Chen, Z. Y., Hasson, T., Kelley, P. M., Schwender, B. J., Schwartz, M. F., Ramakrishnan, M., Kimberling, W. J., Mooseker, M. S., and Corey, D. P. (1996) Molecular Cloning and Domain Structure of Human Myosin-VIIa, the Gene Product Defective in Usher Syndrome 1B. Genomics. 36, 440-448.
13. Delprat, B., Michel, V., Goodyear, R., Yamasaki, Y., Michalski, N., El-Amraoui, A., Perfettini, I., Legrain, P., Richardson, G., Hardelin, J. P., and Petit, C. (2005) Myosin XVa and Whirlin, Two Deafness Gene Products Required for Hair Bundle Growth, are Located at the Stereocilia Tips and Interact Directly. Hum Mol Genet. 14, 401-410.
14. Weber, K. L., Sokac, A. M., Berg, J. S., Cheney, R. E., and Bement, W. M. (2004) A Microtubule-Binding Myosin Required for Nuclear Anchoring and Spindle Assembly. Nature. 431, 325-329.
15. Yonemura, S., Hirao, M., Doi, Y., Takahashi, N., Kondo, T., Tsukita, S., and Tsukita, S. (1998) Ezrin/radixin/moesin (ERM) Proteins Bind to a Positively Charged Amino Acid Cluster in the Juxta-Membrane Cytoplasmic Domain of CD44, CD43, and ICAM-2. J Cell Biol. 140, 885-895.
16. Chishti, A. H., Kim, A. C., Marfatia, S. M., Lutchman, M., Hanspal, M., Jindal, H., Liu, S. C., Low, P. S., Rouleau, G. A., Mohandas, N., Chasis, J. A., Conboy, J. G., Gascard, P., Takakuwa, Y., Huang, S. C., Benz, E. J.,Jr, Bretscher, A., Fehon, R. G., Gusella, J. F., Ramesh, V., Solomon, F., Marchesi, V. T., Tsukita, S., Tsukita, S., and Hoover, K. B. (1998) The FERM Domain: A Unique Module Involved in the Linkage of Cytoplasmic Proteins to the Membrane. Trends Biochem Sci. 23, 281-282.
17. Yu, H., Chen, J. K., Feng, S., Dalgarno, D. C., Brauer, A. W., and Schreiber, S. L. (1994) Structural Basis for the Binding of Proline-Rich Peptides to SH3 Domains. Cell. 76, 933-945.
18. Shupliakov, O., Low, P., Grabs, D., Gad, H., Chen, H., David, C., Takei, K., De Camilli, P., and Brodin, L. (1997) Synaptic Vesicle Endocytosis Impaired by Disruption of Dynamin-SH3 Domain Interactions. Science. 276, 259-263.
19. Anderson, B. L., Boldogh, I., Evangelista, M., Boone, C., Greene, L. A., and Pon, L. A. (1998) The Src Homology Domain 3 (SH3) of a Yeast Type I Myosin, Myo5p, Binds to Verprolin and is Required for Targeting to Sites of Actin Polarization. J Cell Biol. 141, 1357-1370.
20. Sheng, M., and Sala, C. (2001) PDZ Domains and the Organization of Supramolecular Complexes. Annu Rev Neurosci. 24, 1-29.
21. Shearer, A. E., Hildebrand, M. S., Webster, J. A., Kahrizi, K., Meyer, N. C., Jalalvand, K., Arzhanginy, S., Kimberling, W. J., Stephan, D., Bahlo, M., Smith, R. J., and Najmabadi, H. (2009) Mutations in the First MyTH4 Domain of MYO15A are a Common Cause of DFNB3 Hearing Loss. Laryngoscope. 119, 727-733.
22. Prosser, H. M., Rzadzinska, A. K., Steel, K. P., and Bradley, A. (2008) Mosaic Complementation Demonstrates a Regulatory Role for Myosin VIIa in Actin Dynamics of Stereocilia. Mol Cell Biol. 28, 1702-1712.
23. Belyantseva, I. A., Boger, E. T., and Friedman, T. B. (2003) Myosin XVa Localizes to the Tips of Inner Ear Sensory Cell Stereocilia and is Essential for Staircase Formation of the Hair Bundle. Proc Natl Acad Sci U S A. 100, 13958-13963.
24. Rzadzinska, A. K., Schneider, M. E., Davies, C., Riordan, G. P., and Kachar, B. (2004) An Actin Molecular Treadmill and Myosins Maintain Stereocilia Functional Architecture and Self-Renewal. J Cell Biol. 164, 887-897.
25. La Rosa, S., Capella, C., and Lloyd, R. V. (2002) Localization of Myosin XVA in Endocrine Tumors of Gut and Pancreas. Endocr Pathol. 13, 29-37.
26. Lloyd, R. V., Vidal, S., Jin, L., Zhang, S., Kovacs, K., Horvath, E., Scheithauer, B. W., Boger, E. T., Fridell, R. A., and Friedman, T. B. (2001) Myosin XVA Expression in the Pituitary and in Other Neuroendocrine Tissues and Tumors. Am J Pathol. 159, 1375-1382.
27. Mermall, V., Post, P. L., and Mooseker, M. S. (1998) Unconventional Myosins in Cell Movement, Membrane Traffic, and Signal Transduction. Science. 279, 527-533.
28. Baker, J. P., and Titus, M. A. (1997) A Family of Unconventional Myosins from the Nematode Caenorhabditis Elegans. J Mol Biol. 272, 523-535.
29. Etournay, R., Lepelletier, L., Boutet de Monvel, J., Michel, V., Cayet, N., Leibovici, M., Weil, D., Foucher, I., Hardelin, J. P., and Petit, C. (2010) Cochlear Outer Hair Cells Undergo an Apical Circumference Remodeling Constrained by the Hair Bundle Shape. Development. 137, 1373-1383.
30. Fettiplace, R., and Hackney, C. M. (2006) The Sensory and Motor Roles of Auditory Hair Cells. Nat Rev Neurosci. 7, 19-29.
31. Held, N., Smits, B. M., Gockeln, R., Schubert, S., Nave, H., Northrup, E., Cuppen, E., Hedrich, H. J., and Wedekind, D. (2011) A Mutation in Myo15 Leads to Usher-Like Symptoms in LEW/Ztm-ci2 Rats. PLoS One. 6, e15669.
32. Stepanyan, R., Belyantseva, I. A., Griffith, A. J., Friedman, T. B., and Frolenkov, G. I. (2006) Auditory Mechanotransduction in the Absence of Functional Myosin-XVa. J Physiol. 576, 801-808.
|Science Writers||Anne Murray|
|Authors||Jennifer Weatherly Tiana Purrington Bruce Beutler|
|List |< first << previous [record 52 of 74] next >> last >||