Linked Life Data

15226371

Source:http://linkedlifedata.com/resource/pubmed/id/15226371

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 16
pubmed:dateCreated
2004-7-14
pubmed:abstractText
Serum-soluble factors play a dominant role in the activation of the small GTPase RhoA. Cell adhesion also modulates RhoA activity but the effect is modest in the absence of serum. Here, we show that cell adhesion is required for serum-stimulated Rho signal transduction leading to myosin light chain (MLC) phosphorylation. Characterization of Rho-kinase substrates revealed that diphosphorylation of MLC at Thr-18 and Ser-19 (ppMLC(T18/S19)) and phosphorylation of the myosin-binding subunit (MBS) of myosin phosphatase at Thr-853 (pMBS(T853)) were mostly Rho and Rho-kinase dependent in attached fibroblasts. MLC monophosphorylation at Ser-19 (pMLC(S19)) was partially dependent on Rho kinase, whereas phosphorylation of MBS at Thr-696 (pMBS(T696)) and phosphorylation of CPI-17 at Thr-38 (pCPI-17(T38)) were mostly Rho-kinase independent. Cell detachment caused a significant reduction in pMLC(S19) and a more dramatic decrease of ppMLC(T18/S19) without inhibiting RhoA. pMBS(T853), pMBS(T696) and pCPI-17(T38) were not significantly reduced, suggesting that myosin-phosphatase activity was little changed. Cells expressing active RhoA (RhoA(V14)) or Rho-kinase catalytic domain maintained elevated pMBS(T853) upon detachment but failed to support ppMLC(T18/S19), indicating that the ability of Rho kinase to phosphorylate MLC is impaired. Reattachment to immobilized fibronectin resulted in a gradual recovery of Rho-kinase-induced ppMLC(T18/S19) that is absent from the cells attached to poly-L-lysine. The convergence of signals from soluble factors and cell adhesion might therefore occur at the point of MLC phosphorylation, providing an effective mechanism for dynamic control of contractility during cell migration.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
117
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3511-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Disruption of Rho signal transduction upon cell detachment.
pubmed:affiliation
Department of Dermatology, SUNY at Stony Brook, Stony Brook, NY 11794, USA. xiang-dong.ren@sunysb.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't