Unconventional myosin ID is expressed in myelinating oligodendrocytes

2014 ◽  
Vol 92 (10) ◽  
pp. 1286-1294 ◽  
Author(s):  
Reiji Yamazaki ◽  
Tomoko Ishibashi ◽  
Hiroko Baba ◽  
Yoshihide Yamaguchi
Keyword(s):  
Unconventional Myosin

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.

Expression of Unconventional Myosin VI in Oligodendrocytes

2017 ◽  
Vol 42 (12) ◽  
pp. 3372-3381 ◽  
Author(s):  
Reiji Yamazaki ◽  
Tomoko Ishibashi ◽  
Hiroko Baba ◽  
Yoshihide Yamaguchi
Keyword(s):  
Myosin Vi ◽  
Unconventional Myosin

scholarly journals Class VI Unconventional Myosin is Required for Spermatogenesis inDrosophila

1999 ◽  
Vol 10 (12) ◽  
pp. 4341-4353 ◽  
Author(s):  
Jennifer L. Hicks ◽  
Wu-Min Deng ◽  
Aaron D. Rogat ◽  
Kathryn G. Miller ◽  
Mary Bownes
Keyword(s):  
Male Sterility ◽  
Germ Line ◽  
Critical Role ◽  
Leading Edge ◽  
Cytoskeletal Proteins ◽  
Loss Of Function ◽  
Unconventional Myosin ◽  
Membrane Reorganization ◽  
Cytoplasmic Bridges ◽  
Mitosis And Meiosis

We have identified partial loss of function mutations in class VI unconventional myosin, 95F myosin, which results in male sterility. During spermatogenesis the germ line precursor cells undergo mitosis and meiosis to form a bundle of 64 spermatids. The spermatids remain interconnected by cytoplasmic bridges until individualization. The process of individualization involves the formation of a complex of cytoskeletal proteins and membrane, the individualization complex (IC), around the spermatid nuclei. This complex traverses the length of each spermatid resolving the shared membrane into a single membrane enclosing each spermatid. We have determined that 95F myosin is a component of the IC whose function is essential for individualization. In wild-type testes, 95F myosin localizes to the leading edge of the IC. Two independent mutations in 95F myosin reduce the amount of 95F myosin in only a subset of tissues, including the testes. This reduction of 95F myosin causes male sterility as a result of defects in spermatid individualization. Germ line transformation with the 95F myosin heavy chain cDNA rescues the male sterility phenotype. IC movement is aberrant in these 95F myosin mutants, indicating a critical role for 95F myosin in IC movement. This report is the first identification of a component of the IC other than actin. We propose that 95F myosin is a motor that participates in membrane reorganization during individualization.

MYO1, a Novel, Unconventional Myosin Gene Affects Endocytosis and Macronuclear Elongation in Tetrahymena thermophila

2000 ◽  
Vol 47 (6) ◽  
pp. 561-568 ◽  
Author(s):  
SELWYN A. WILLIAMS ◽  
ROLAND E. HOSEIN ◽  
JORGE A. GARCES ◽  
R. H. GAVIN
Keyword(s):  
Tetrahymena Thermophila ◽  
Unconventional Myosin

scholarly journals Uncoated Endocytic Vesicles Require the Unconventional Myosin, Myo6, for Rapid Transport through Actin Barriers

2004 ◽  
Vol 15 (5) ◽  
pp. 2253-2263 ◽  
Author(s):  
Laura Aschenbrenner ◽  
Samia N. Naccache ◽  
Tama Hasson
Keyword(s):  
Epithelial Cells ◽  
Motor Activity ◽  
Time Lapse ◽  
Early Endosome ◽  
Physical Barrier ◽  
Unconventional Myosin ◽  
Time Lapse Microscopy ◽  
Rapid Transport ◽  
Endocytic Vesicles

After clathrin-mediated endocytosis, clathrin removal yields an uncoated vesicle population primed for fusion with the early endosome. Here we present the first characterization of uncoated vesicles and show that myo6, an unconventional myosin, functions to move these vesicles out of actin-rich regions found in epithelial cells. Time-lapse microscopy revealed that myo6-associated uncoated vesicles were motile and exhibited fusion and stretching events before endosome delivery, processes that were dependent on myo6 motor activity. In the absence of myo6 motor activity, uncoated vesicles remained trapped in the actin mesh, where they exhibited Brownian-like motion. Exit from the actin mesh occurred by a slow diffusion-based mechanism, delaying transferrin trafficking to the early endosome. Expression of a myo6 mutant that bound tightly to F-actin produced immobilized vesicles and blocked trafficking. Depolymerization of the actin cytoskeleton rescued this block and specifically accelerated transferrin delivery to the early endosome without affecting earlier steps in endocytosis. Therefore actin is a physical barrier impeding uncoated vesicle trafficking, and myo6 is recruited to move the vesicles through this barrier for fusion with the early endosome.

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