Regulation of Class I and Class II Myosins by Heavy Chain Phosphorylation

Brzeska, Hanna; Korn, Edward D.

doi:10.1074/jbc.271.29.16983

Cited by 93 publications

(64 citation statements)

References 64 publications

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“…In various eukaryotes, phosphorylation or dephosphorylation of myosin has been well documented as a regulatory mechanism of myosin II Brzeska and Korn, 1996;Kamm and Stull, 2001;Loo and Balasubramanian, 2008). Notably, it has been reported that the phosphorylation of the Cdc4 protein is not required for cytokinesis (McCollum et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

“…Type II myosin consists of a dimer comprising two heavy chains, each having two associated proteins: the essential light chain and regulatory light chain (Guertin et al, 2002). In various eukaryotes, the phosphorylation of both the heavy and light chains of myosin has been well documented as a primary means of activating myosin II, which is known to be crucial for cytokinesis Brzeska and Korn, 1996;Kamm and Stull, 2001).…”

Section: Introductionmentioning

confidence: 99%

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Role of the RNA-binding Protein Nrd1 and Pmk1 Mitogen-activated Protein Kinase in the Regulation of Myosin mRNA Stability in Fission Yeast

Satoh

Morita

Takada

et al. 2009

MBoC

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Myosin II is an essential component of the actomyosin contractile ring and plays a crucial role in cytokinesis by generating the forces necessary for contraction of the actomyosin ring. Cdc4 is an essential myosin II light chain in fission yeast and is required for cytokinesis. In various eukaryotes, the phosphorylation of myosin is well documented as a primary means of activating myosin II, but little is known about the regulatory mechanisms of Cdc4. Here, we isolated Nrd1, an RNA-binding protein with RNA-recognition motifs, as a multicopy suppressor of cdc4 mutants. Notably, we demonstrated that Nrd1 binds and stabilizes Cdc4 mRNA, thereby suppressing the cytokinesis defects of the cdc4 mutants. Importantly, Pmk1 mitogen-activated protein kinase (MAPK) directly phosphorylates Nrd1, thereby negatively regulating the binding activity of Nrd1 to Cdc4 mRNA. Consistently, the inactivation of Pmk1 MAPK signaling, as well as Nrd1 overexpression, stabilized the Cdc4 mRNA level, thereby suppressing the cytokinesis defects associated with the cdc4 mutants. In addition, we demonstrated the cell cycle-dependent regulation of Pmk1/Nrd1 signaling. Together, our results indicate that Nrd1 plays a role in the regulation of Cdc4 mRNA stability; moreover, our study is the first to demonstrate the posttranscriptional regulation of myosin expression by MAPK signaling.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Role of the RNA-binding Protein Nrd1 and Pmk1 Mitogen-activated Protein Kinase in the Regulation of Myosin mRNA Stability in Fission Yeast

Satoh

Morita

Takada

et al. 2009

MBoC

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“…The regulation of myosin II function by tail phosphorylation has hitherto only been described in amoebae (reviewed in Brzeska and Korn, 1996). In Acanthamoeba, myosin II activity is negatively regulated by phosphorylation of a C-terminal, nonhelical region of its heavy chain (Collins et al, 1982;Ganguly et al, 1992).…”

Section: Discussionmentioning

confidence: 99%

Localization of Fission Yeast Type II Myosin, Myo2, to the Cytokinetic Actin Ring Is Regulated by Phosphorylation of a C-Terminal Coiled-Coil Domain and Requires a Functional Septation Initiation Network

Mulvihill

Barretto

Hyams

2001

MBoC

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Myo2 truncations fused to green fluorescent protein (GFP) defined a C-terminal domain essential for the localization of Myo2 to the cytokinetic actin ring (CAR). The localization domain contained two predicted phosphorylation sites. Mutation of serine 1518 to alanine (S1518A) abolished Myo2 localization, whereas Myo2 with a glutamic acid at this position (S1518E) localized to the CAR. GFP-Myo2 formed rings in the septation initiation kinase (SIN) mutant cdc7-24 at 25°C but not at 36°C. GFP-Myo2S1518E rings persisted at 36°C incdc7-24 but not in another SIN kinase mutant,sid2-250. To further examine the relationship between Myo2 and the SIN pathway, the chromosomal copy ofmyo2 + was fused to GFP (strainmyo2-gc). Myo2 ring formation was abolished in the double mutants myo2-gc cdc7.24 and myo2-gc sid2-250 at the restrictive temperature. In contrast, activation of the SIN pathway in the double mutant myo2-gc cdc16-116 resulted in the formation of Myo2 rings which subsequently collapsed at 36°C. We conclude that the SIN pathway that controls septation in fission yeast also regulates Myo2 ring formation and contraction. Cdc7 and Sid2 are involved in ring formation, in the case of Cdc7 by phosphorylation of a single serine residue in the Myo2 tail. Other kinases and/or phosphatases may control ring contraction.

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“…Conidia of MYOA null cells swell and undergo nuclear division but do not initiate hyphal growth and ultimately die (8). Importantly, MYOA is one of a small subset of myosins (class I myosins of A. nidulans, Acanthamoeba castellanii, Dictyostelium discoideum, Saccharomyces cerevisiae, Schizosaccharomyces pombe, and the eight class VI myosins that have been sequenced) that have either a serine or threonine residue in the motor domain at a position [the TEDS site (10), Ser-371 in MYOA] in an actinbinding surface loop (11) where all other myosins contain either an aspartate or glutamate residue (10,12,13). The actindependent MgATPase and in vitro motility activities of A. castellanii (14) and D. discoideum (15) class I myosins are regulated by phosphorylation of the TEDS-site serine or threonine by p21-activated kinases (16,17).…”

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confidence: 99%

Myosin I mutants with only 1% of wild-type actin-activated MgATPase activity retain essentialin vivofunction(s)

Liu

Osherov

Yamashita

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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The single class I myosin (MYOA) of Aspergillus nidulans is essential for hyphal growth. It is generally assumed that the functions of all myosins depend on their actin-activated MgATPase activity. Here we show that MYOA mutants with no more than 1% of the actin-activated MgATPase activity of wild-type MYOA in vitro and no detectable in vitro motility activity can support fungal cell growth, albeit with a delay in germination time and a reduction in hyphal elongation. From these and other data, we conclude that the essential role(s) of myosin I in A. nidulans is probably structural, requiring little, if any, actin-activated MgATPase or motor activity, which have long been considered the defining characteristics of the myosin family.

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Regulation of Class I and Class II Myosins by Heavy Chain Phosphorylation

Cited by 93 publications

References 64 publications

Role of the RNA-binding Protein Nrd1 and Pmk1 Mitogen-activated Protein Kinase in the Regulation of Myosin mRNA Stability in Fission Yeast

Role of the RNA-binding Protein Nrd1 and Pmk1 Mitogen-activated Protein Kinase in the Regulation of Myosin mRNA Stability in Fission Yeast

Localization of Fission Yeast Type II Myosin, Myo2, to the Cytokinetic Actin Ring Is Regulated by Phosphorylation of a C-Terminal Coiled-Coil Domain and Requires a Functional Septation Initiation Network

Myosin I mutants with only 1% of wild-type actin-activated MgATPase activity retain essentialin vivofunction(s)

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