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PAK kinases are directly coupled to the PIX family of nucleotide exchange factors.
TLDR
The results suggest a role for PIX in Cdc42-to-Rac1 signaling, involving the PIX/PAK complex, and a new class of Rho-p21 guanine nucleotide exchange factor binding tightly through its N-terminal SH3 domain to a conserved proline-rich PAK sequence with a Kd of 24 nM.
Myotonic Dystrophy Kinase-Related Cdc42-Binding Kinase Acts as a Cdc42 Effector in Promoting Cytoskeletal Reorganization
TLDR
The results suggest that MRCKα may act as a downstream effector of Cdc42 in cytoskeletal reorganization, and is isolated two related novel brain kinases whose p21-binding domains resemble that of PAK whereas the kinase domains resemble the myotonic dystrophy kinase-related ROK.
A Drosophila homolog of the Rac- and Cdc42-activated serine/threonine kinase PAK is a potential focal adhesion and focal complex protein that colocalizes with dynamic actin structures
TLDR
It is proposed that DPAK may be regulating the cytoskeleton through its association with focal adhesions and focal complexes and may be participating with DRacA in a c-Jun amino-terminal kinase signaling pathway recently demonstrated to be required for dorsal closure.
Phosphorylation of a Novel Myosin Binding Subunit of Protein Phosphatase 1 Reveals a Conserved Mechanism in the Regulation of Actin Cytoskeleton*
TLDR
Substrate screening in various tissues uncovered two major substrates, p130 and p85, for MRCKα-kinase, providing further evidence that phosphorylation of a myosin binding subunit protein by specific kinases confers conformational changes in a highly conserved region that plays an essential role in the regulation of its catalytic subunit activities.
A Tripartite Complex Containing MRCK Modulates Lamellar Actomyosin Retrograde Flow
TLDR
The promotion of persistent protrusive activity and inhibition of cell motility by the respective expression of wild-type and dominant-negative mutant components of the MRCK complex show it to be crucial to cell protrusion and migration.
Actin-binding and Cell Proliferation Activities of Angiomotin Family Members Are Regulated by Hippo Pathway-mediated Phosphorylation*
TLDR
The results collectively suggest that the Hippo pathway negatively regulates the actin-binding activity of Amot family members through direct phosphorylation.
Phosphorylation of Myosin Phosphatase Targeting Subunit 3 (MYPT3) and Regulation of Protein Phosphatase 1 by Protein Kinase A*
TLDR
It is shown that myosin phosphatase targeting subunit 3 can be a substrate for protein kinase A (PKA) and a novel mechanism for the phosphorylation of MYPT3 by PKA and activation of the catalytic activity through direct interaction of a central region of MyPT3 with its N-terminal region is proposed.
Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase‐related Cdc42‐binding kinase
TLDR
MLCK phosphorylates MLC by protein kinase assay (View interaction) and indicates phosphorylation of MLCK by Protein kinase A in the presence of Na6(CO3)(SO4), Na2SO4, Na2CO3, and Na2O2.
ACK Family Tyrosine Kinase Activity Is a Component of Dcdc42 Signaling during Dorsal Closure in Drosophila melanogaster
TLDR
Expression of wild-type and kinase-dead DACK transgenes in embryos, and in the developing wing and eye, reveals that ACK family tyrosine kinase activity is involved in a range of developmental events similar to that of Dcdc42.
Intermolecular and Intramolecular Interactions Regulate Catalytic Activity of Myotonic Dystrophy Kinase-Related Cdc42-Binding Kinase α
TLDR
Evidence is provided that the N terminus-mediated dimerization and activation of MRCK and the negative autoregulatory kinase–distal CC interaction are two mutually exclusive events that tightly regulate the catalytic state of the kinase.
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