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Rho-regulated Myosin Phosphatase Establishes The Level Of Protrusive - Dev Biologists
Get Rho-regulated Myosin Phosphatase Establishes The Level Of Protrusive - Dev Biologists
Sh gastrulation Douglas C. Weiser*, Richard H. Row and David Kimelman Rho-dependent amoeboid cell movement is a crucial mechanism in both tumor cell invasion and morphogenetic cell movements during fish gastrulation. Amoeboid movement is characterized by relatively non-polarized cells displaying a high level of bleb-like protrusions. During gastrulation, zebrafish mesodermal cells undergo a series of conversions from amoeboid cell behaviors to more mesenchymal and finally highly polarized and.
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2002 FAQ
Abstract. Myosin light chain kinase (MLCK) plays a central role in regulating the actin-myosin interaction of smooth muscle. MLCK phosphorylates the light chain of myosin in the presence of Ca2+ and calmodulin (CaM) thereby activating myosin so that it can interact with actin.
This dephosphorylation reaction occurs in smooth muscle tissue and initiates the relaxation process of the muscle cells. Thus, myosin phosphatase undoes the muscle contraction process initiated by myosin light-chain kinase.
This dephosphorylation reaction occurs in smooth muscle tissue and initiates the relaxation process of the muscle cells. Thus, myosin phosphatase undoes the muscle contraction process initiated by myosin light-chain kinase.
MYPT1 binds the catalytic subunit of type 1 phosphatase, δ isoform, and also acts as an interactive platform for many other proteins. A key reaction for MP is with phosphorylated myosin II and the first process shown to be regulated by MP was contractile activity of smooth muscle.
A phosphatase is an enzyme that removes a phosphate group from a protein. Together, these two families of enzymes act to modulate the activities of the proteins in a cell, often in response to external stimuli.
Myosin light chain phosphatase (MLCP) is responsible for the dephosphorylation of the regulatory light chain (RLC) of the motor protein myosin-II, and so negatively regulates actomyosin-based contractility.
(A) Active MLCP dephosphorylates the light chain of myosin (MLC20) at the Ser19 residue and induces smooth muscle relaxation. (B) Signaling pathway mediated by RhoA kinase (ROCK). Several agonists activate the RhoA–ROCK pathway. RhoA activation is dependent on GTP and can induce ROCK activity.
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phosphorylation
mesodermal
morphant
Blebbing
mRNA
2008
2002
protrusive
biol
phenotype
Weiser
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