scholarly journals The fission yeast Chs2 protein interacts with the type-II myosin Myo3p and is required for the integrity of the actomyosin ring

2006 ◽  
Vol 119 (13) ◽  
pp. 2768-2779 ◽  
Author(s):  
R. Martin-Garcia
Keyword(s):  
Fission Yeast ◽  
Type Ii ◽  
Type Ii Myosin

Type II myosin involved in cytokinesis in the fission yeast,Schizosaccharomyces pombe

1997 ◽  
Vol 38 (4) ◽  
pp. 385-396 ◽  
Author(s):  
Karen M. May ◽  
Felicity Z. Watts ◽  
Nic Jones ◽  
Jeremy S. Hyams
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Type Ii ◽  
Type Ii Myosin

Identification of Myo3, a second type-II myosin heavy chain in the fission yeast Schizosaccharomyces pombe

FEBS Letters ◽  
1997 ◽  
Vol 420 (2-3) ◽  
pp. 161-166 ◽  
Author(s):  
Fumio Motegi ◽  
Kentaro Nakano ◽  
Chikako Kitayama ◽  
Masayuki Yamamoto ◽  
Issei Mabuchi
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Myosin Heavy Chain ◽  
Fission Yeast ◽  
Heavy Chain ◽  
Type Ii ◽  
Type Ii Myosin

Fission yeast Rng3p: an UCS-domain protein that mediates myosin II assembly during cytokinesis

2000 ◽  
Vol 113 (13) ◽  
pp. 2421-2432 ◽  
Author(s):  
K.C. Wong ◽  
N.I. Naqvi ◽  
Y. Iino ◽  
M. Yamamoto ◽  
M.K. Balasubramanian
Keyword(s):  
Fission Yeast ◽  
Fluorescent Protein ◽  
Type Ii ◽  
Division Site ◽  
Ring Assembly ◽  
Medial Cortex ◽  
Late Step ◽  
Green Fluorescent ◽  
Type Ii Myosin

Cell division in many eukaryotes, including the fission yeast Schizosaccharomyces pombe, utilizes a contractile actomyosin ring. In S. pombe, the actomyosin ring is assembled at the medial cortex upon entry into mitosis and constricts at the end of anaphase to guide the centripetal deposition of the septum. Despite identification of several structural components essential for actomyosin ring assembly, the interdependencies between these gene-products in the process of ring assembly are unknown. This study investigates the role of Rng3p, a member of the UCS-domain containing protein family (Unc-45p, Cro1p, She4p), in actomyosin ring assembly. Null mutants in rng3 resemble deletion mutants in the type II myosin heavy chain (myo2) and rng3(ts) mutants show strong negative interactions with the myo2-E1 mutant, suggesting that Rng3p is involved in modulating aspects of type II myosin function. Interestingly, a green fluorescent protein (GFP) tagged Rng3p fusion is detected at the division site in the myo2-E1 mutant, but not in other myo2-alleles, wild-type cells or in 18 other cytokinesis mutants. Assembly and maintenance of Rng3p at the division site in the myo2-E1 mutant requires F-actin. Rng3p is also required for the proper assembly of Myo2p and F-actin into a functional actomyosin ring but is not necessary for their accumulation at the division site. We conclude that Rng3p is a novel component of the F-actin cytoskeleton essential for a late step in actomyosin ring assembly and that it might monitor some aspect of type II myosin assembly during actomyosin ring construction.

scholarly journals Pxl1p, a Paxillin-related Protein, Stabilizes the Actomyosin Ring during Cytokinesis in Fission Yeast

2008 ◽  
Vol 19 (4) ◽  
pp. 1680-1692 ◽  
Author(s):  
Wanzhong Ge ◽  
Mohan K. Balasubramanian
Keyword(s):  
Actin Cytoskeleton ◽  
Fission Yeast ◽  
Genetic Interactions ◽  
Type Ii ◽  
Related Protein ◽  
Lim Domain ◽  
Genetic Studies ◽  
Late Anaphase ◽  
Ring Constriction ◽  
Type Ii Myosin

Paxillins are a family of conserved LIM domain-containing proteins that play important roles in the function and integrity of the actin cytoskeleton. Although paxillins have been extensively characterized by cell biological and biochemical approaches, genetic studies are relatively scarce. Here, we identify and characterize a paxillin-related protein Pxl1p in the fission yeast Schizosaccharomyces pombe. Pxl1p is a component of the fission yeast actomyosin ring, a structure that is essential for cytokinesis. Cells deleted for pxl1 display a novel phenotype characterized by a splitting of the actomyosin ring in late anaphase, leading to the formation of two rings of which only one undergoes constriction. In addition, the rate of actomyosin ring constriction is slower in the absence of Pxl1p. pxl1Δ mutants display strong genetic interactions with mutants defective in IQGAP-related protein Rng2p and mutants defective in components of the fission yeast type II myosin machinery. Collectively, these results suggest that Pxl1p might cooperate with type II myosin and Rng2p-IQGAP to regulate actomyosin ring constriction as well as to maintain its integrity during constriction.

scholarly journals F-actin and a Type-II Myosin Are Required for Efficient Clustering of the ER Stress Sensor Ire1

2013 ◽  
Vol 38 (2) ◽  
pp. 135-143 ◽  
Author(s):  
Yuki Ishiwata-Kimata ◽  
Yo-hei Yamamoto ◽  
Ken Takizawa ◽  
Kenji Kohno ◽  
Yukio Kimata
Keyword(s):  
Er Stress ◽  
Type Ii ◽  
Stress Sensor ◽  
Type Ii Myosin

scholarly journals Aim44p regulates phosphorylation of Hof1p to promote contractile ring closure during cytokinesis in budding yeast

2014 ◽  
Vol 25 (6) ◽  
pp. 753-762 ◽  
Author(s):  
Dana M. Alessi Wolken ◽  
Joseph McInnes ◽  
Liza A. Pon
Keyword(s):  
Cell Division ◽  
Protein Product ◽  
Ring Closure ◽  
Type Ii ◽  
Contractile Ring ◽  
Double Ring ◽  
Mother And Daughter ◽  
Associated Proteins ◽  
And Function ◽  
Type Ii Myosin

Whereas actomyosin and septin ring organization and function in cytokinesis are thoroughly described, little is known regarding the mechanisms by which the actomyosin ring interacts with septins and associated proteins to coordinate cell division. Here we show that the protein product of YPL158C, Aim44p, undergoes septin-dependent recruitment to the site of cell division. Aim44p colocalizes with Myo1p, the type II myosin of the contractile ring, throughout most of the cell cycle. The Aim44p ring does not contract when the actomyosin ring closes. Instead, it forms a double ring that associates with septin rings on mother and daughter cells after cell separation. Deletion of AIM44 results in defects in contractile ring closure. Aim44p coimmunoprecipitates with Hof1p, a conserved F-BAR protein that binds both septins and type II myosins and promotes contractile ring closure. Deletion of AIM44 results in a delay in Hof1p phosphorylation and altered Hof1p localization. Finally, overexpression of Dbf2p, a kinase that phosphorylates Hof1p and is required for relocalization of Hof1p from septin rings to the contractile ring and for Hof1p-triggered contractile ring closure, rescues the cytokinesis defect observed in aim44∆ cells. Our studies reveal a novel role for Aim44p in regulating contractile ring closure through effects on Hof1p.

Relationships between maximal strength, muscle size, and myosin heavy chain isoform composition and postactivation potentiation

2016 ◽  
Vol 41 (5) ◽  
pp. 491-497 ◽  
Author(s):  
Laurent B. Seitz ◽  
Gabriel S. Trajano ◽  
G. Gregory Haff ◽  
Charles C.L.S. Dumke ◽  
James J. Tufano ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Human Skeletal Muscle ◽  
Knee Extensor ◽  
Type Ii ◽  
Postactivation Potentiation ◽  
Test Protocol ◽  
Extensor Torque ◽  
Type Ii Myosin

The purpose of this study was to examine the relationships between maximal voluntary postactivation potentiation (PAP) and maximal knee extensor torque, quadriceps cross-sectional area (CSA) and volume, and type II myosin heavy chain (MHC) isoform percentage in human skeletal muscle. Thirteen resistance-trained men completed a test protocol consisting of 2 isokinetic knee extensions at 180°·s–1 performed before and 1, 4, 7, and 10 min after the completion of 4 maximal knee extensions at 60°·s–1 (i.e., a conditioning activity (CA)). Magnetic resonance imaging and muscle microbiopsy procedures were completed on separate days to assess quadriceps CSA and volume and MHC isoform content. Maximal voluntary PAP response was assessed as the ratio of the highest knee extensor torques measured before and after the CA. There were large to very large correlations between maximal voluntary PAP response and maximal knee extensor torque (r = 0.62) and quadriceps CSA (r = 0.68) and volume (r = 0.63). Nonetheless, these correlations were not statistically significant after adjusting for the influence of type II MHC percentage using partial correlation analysis. By contrast, the strongest correlation was observed for type II MHC percentage (r = 0.77), and this correlation remained significant after adjusting for the other variables. Maximal voluntary PAP response is strongly correlated with maximal knee extensor torque and quadriceps CSA and volume, but is mostly clearly associated with the type II myosin isoform percentage in human skeletal muscle.

Type II myosin gene in Fusarium graminearum is required for septation, development, mycotoxin biosynthesis and pathogenicity

2013 ◽  
Vol 54 ◽  
pp. 60-70 ◽  
Author(s):  
Bo Song ◽  
He-Ping Li ◽  
Jing-Bo Zhang ◽  
Jian-Hua Wang ◽  
An-Dong Gong ◽  
...  
Keyword(s):  
Fusarium Graminearum ◽  
Type Ii ◽  
Mycotoxin Biosynthesis ◽  
Type Ii Myosin
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