scholarly journals The unconventional myosin-VIIa associates with lysosomes

2005 ◽  
Vol 62 (1) ◽  
pp. 13-26 ◽  
Author(s):  
Lily E. Soni ◽  
Carmen M. Warren ◽  
Cecilia Bucci ◽  
Dana J. Orten ◽  
Tama Hasson
Keyword(s):  
Unconventional Myosin ◽  
Myosin Viia

scholarly journals Unconventional Myosin VIIA Is a Novel A-kinase-anchoring Protein

2000 ◽  
Vol 275 (38) ◽  
pp. 29654-29659 ◽  
Author(s):  
Polonca Küssel-Andermann ◽  
Aziz El-Amraoui ◽  
Saaid Safieddine ◽  
Jean-Pierre Hardelin ◽  
Sylvie Nouaille ◽  
...  
Keyword(s):  
Unconventional Myosin ◽  
Anchoring Protein ◽  
Myosin Viia

scholarly journals Unconventional Myosins in Inner-Ear Sensory Epithelia

1997 ◽  
Vol 137 (6) ◽  
pp. 1287-1307 ◽  
Author(s):  
Tama Hasson ◽  
Peter G. Gillespie ◽  
Jesus A. Garcia ◽  
Richard B. MacDonald ◽  
Yi-dong Zhao ◽  
...  
Keyword(s):  
Inner Ear ◽  
Hair Cells ◽  
Actin Filaments ◽  
Structural Integrity ◽  
Myosin Vi ◽  
Cortical Actin ◽  
Unconventional Myosin ◽  
Myosin Isozymes ◽  
Cuticular Plate ◽  
Myosin Viia

To understand how cells differentially use the dozens of myosin isozymes present in each genome, we examined the distribution of four unconventional myosin isozymes in the inner ear, a tissue that is particularly reliant on actin-rich structures and unconventional myosin isozymes. Of the four isozymes, each from a different class, three are expressed in the hair cells of amphibia and mammals. In stereocilia, constructed of cross-linked F-actin filaments, myosin-Iβ is found mostly near stereociliary tips, myosin-VI is largely absent, and myosin-VIIa colocalizes with crosslinks that connect adjacent stereocilia. In the cuticular plate, a meshwork of actin filaments, myosin-Iβ is excluded, myosin-VI is concentrated, and modest amounts of myosin-VIIa are present. These three myosin isozymes are excluded from other actin-rich domains, including the circumferential actin belt and the cortical actin network. A member of a fourth class, myosin-V, is not expressed in hair cells but is present at high levels in afferent nerve cells that innervate hair cells. Substantial amounts of myosins-Iβ, -VI, and -VIIa are located in a pericuticular necklace that is largely free of F-actin, squeezed between (but not associated with) actin of the cuticular plate and the circumferential belt. Our localization results suggest specific functions for three hair-cell myosin isozymes. As suggested previously, myosin-Iβ probably plays a role in adaptation; concentration of myosin-VI in cuticular plates and association with stereociliary rootlets suggest that this isozyme participates in rigidly anchoring stereocilia; and finally, colocalization with cross-links between adjacent stereocilia indicates that myosin-VIIa is required for the structural integrity of hair bundles.

scholarly journals Unconventional myosin VIIA promotes melanoma progression

2018 ◽  
Vol 131 (4) ◽  
pp. jcs209924 ◽  
Author(s):  
Yuqing Liu ◽  
Xiaofan Wei ◽  
Lizhao Guan ◽  
Sidi Xu ◽  
Yang Yuan ◽  
...  
Keyword(s):  
Unconventional Myosin ◽  
Melanoma Progression ◽  
Myosin Viia

Molecular Genetic Dissection of Mouse Unconventional Myosin-VA: Tail Region Mutations

Genetics ◽  
1998 ◽  
Vol 148 (4) ◽  
pp. 1963-1972 ◽  
Author(s):  
Jian-Dong Huang ◽  
Valerie Mermall ◽  
Marjorie C Strobel ◽  
Liane B Russell ◽  
Mark S Mooseker ◽  
...  
Keyword(s):  
Coat Color ◽  
Molecular Genetic ◽  
Genetic Dissection ◽  
Rt Pcr ◽  
Tail Region ◽  
Unconventional Myosin ◽  
Myosin Va ◽  
Cell Type Specific ◽  
Extensive Collection ◽  
Tail Function

AbstractWe used an RT-PCR-based sequencing approach to identify the mutations responsible for 17 viable dilute alleles, a mouse-coat-color locus encoding unconventional myosin-VA. Ten of the mutations mapped to the MyoVA tail and are reported here. These mutations represent the first extensive collection of tail mutations reported for any unconventional mammalian myosin. They identify sequences important for tail function and identify domains potentially involved in cargo binding and/or proper folding of the MyoVA tail. Our results also provide support for the notion that different myosin tail isoforms produced by alternative splicing encode important cell-type-specific functions.

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
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