Structure of MyTH4-FERM Domains in Myosin VIIa Tail Bound to Cargo

Science ◽  
2011 ◽  
Vol 331 (6018) ◽  
pp. 757-760 ◽  
Author(s):  
L. Wu ◽  
L. Pan ◽  
Z. Wei ◽  
M. Zhang
Keyword(s):  
Myosin Viia ◽  
Tail Bound

scholarly journals Impacts of Usher Syndrome Type IB Mutations on Human Myosin VIIa Motor Function†

Biochemistry ◽  
2008 ◽  
Vol 47 (36) ◽  
pp. 9505-9513 ◽  
Author(s):  
Shinya Watanabe ◽  
Nobuhisa Umeki ◽  
Reiko Ikebe ◽  
Mitsuo Ikebe
Keyword(s):  
Motor Function ◽  
Usher Syndrome ◽  
Syndrome Type ◽  
Myosin Viia ◽  
Usher Syndrome Type

Identification and molecular modelling of a mutation in the motor head domain of myosin VIIA in a family with autosomal dominant hearing impairment (DFNA11)

2004 ◽  
Vol 115 (2) ◽  
pp. 149-156 ◽  
Author(s):  
Mirjam W. J. Luijendijk ◽  
Erwin van Wijk ◽  
Anne M. L. C. Bischoff ◽  
Elmar Krieger ◽  
Patrick L. M. Huygen ◽  
...  
Keyword(s):  
Hearing Impairment ◽  
Molecular Modelling ◽  
Autosomal Dominant ◽  
Head Domain ◽  
Myosin Viia ◽  
Motor Head

Shaker-1 mutations reveal roles for myosin VIIA in both development and function of cochlear hair cells

Development ◽  
1998 ◽  
Vol 125 (4) ◽  
pp. 557-566 ◽  
Author(s):  
T. Self ◽  
M. Mahony ◽  
J. Fleming ◽  
J. Walsh ◽  
S.D. Brown ◽  
...  
Keyword(s):  
Hair Cell ◽  
Hair Cells ◽  
Usher Syndrome ◽  
Orthologous Gene ◽  
Cell Development ◽  
Cochlear Hair Cells ◽  
Cochlear Hair Cell ◽  
Show Evidence ◽  
Myosin Viia ◽  
And Function

The mouse shaker-1 locus, Myo7a, encodes myosin VIIA and mutations in the orthologous gene in humans cause Usher syndrome type 1B or non-syndromic deafness. Myo7a is expressed very early in sensory hair cell development in the inner ear. We describe the effects of three mutations on cochlear hair cell development and function. In the Myo7a816SB and Myo7a6J mutants, stereocilia grow and form rows of graded heights as normal, but the bundles become progressively more disorganised. Most of these mutants show no gross electrophysiological responses, but some did show evidence of hair cell depolarisation despite the disorganisation of their bundles. In contrast, the original shaker-1 mutants, Myo7ash1, had normal early development of stereocilia bundles, but still showed abnormal cochlear responses. These findings suggest that myosin VIIA is required for normal stereocilia bundle organisation and has a role in the function of cochlear hair cells.

scholarly journals Myosin VIIA Is Required for Aminoglycoside Accumulation in Cochlear Hair Cells

1997 ◽  
Vol 17 (24) ◽  
pp. 9506-9519 ◽  
Author(s):  
G. P. Richardson ◽  
A. Forge ◽  
C. J. Kros ◽  
J. Fleming ◽  
S. D. M. Brown ◽  
...  
Keyword(s):  
Hair Cells ◽  
Cochlear Hair Cells ◽  
Myosin Viia

Myosin VIIA is specifically associated with calmodulin and microtubule-associated protein-2B (MAP-2B)

2001 ◽  
Vol 354 (2) ◽  
pp. 267-274 ◽  
Author(s):  
Penio T. TODOROV ◽  
Rachel E. HARDISTY ◽  
Steve D. M. BROWN
Keyword(s):  
Binding Sites ◽  
Strong Association ◽  
Mouse Kidney ◽  
Scatchard Analysis ◽  
Tail Region ◽  
Immunoblotting Analysis ◽  
Kd Values ◽  
Myosin Viia

Myosin VIIA is a motor molecule with a conserved head domain and tail region unique to myosin VIIA, which probably defines its unique function in vivo. In an attempt to further characterize myosin VIIA function we set out to identify molecule(s) that specifically associate with it. We demonstrate that 17 and 55kDa proteins from mouse kidney and cochlea co-purify with myosin VIIA on affinity columns carrying immobilized anti-myosin VIIA antibody. N-terminal sequencing and immunoblotting analysis identified the 17kDa protein as calmodulin, whereas MS and immunoblotting analysis identified the 55kDa protein as microtubule-associated protein-2B (MAP-2B). Myosin VIIA can also be co-immunoprecipitated from kidney homogenate using anti-calmodulin or anti-MAP2 (recognizing isoforms 2A and 2B) antibodies, confirming the strong association between calmodulin and myosin VIIA and between MAP-2B and myosin VIIA. Myosin VIIA binds to calmodulin with an apparent Kd of 10-9 M. Scatchard analysis of the binding of myosin VIIA to MAP-2B provided evidence for two binding sites, with Kd values of 10-10 and 10-9 M, which have been mapped to medial and C-terminal tail domains of myosin VIIA. The characterization of the interaction of calmodulin and MAP-2B with myosin VIIA provides new insights into the function of myosin VIIA.

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