| pubmed-article:18613116 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18613116 | lifeskim:mentions | umls-concept:C1366894 | lld:lifeskim |
| pubmed-article:18613116 | lifeskim:mentions | umls-concept:C0887870 | lld:lifeskim |
| pubmed-article:18613116 | lifeskim:mentions | umls-concept:C0007608 | lld:lifeskim |
| pubmed-article:18613116 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
| pubmed-article:18613116 | lifeskim:mentions | umls-concept:C0059239 | lld:lifeskim |
| pubmed-article:18613116 | lifeskim:mentions | umls-concept:C0135575 | lld:lifeskim |
| pubmed-article:18613116 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:18613116 | lifeskim:mentions | umls-concept:C1158884 | lld:lifeskim |
| pubmed-article:18613116 | lifeskim:mentions | umls-concept:C0243127 | lld:lifeskim |
| pubmed-article:18613116 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:18613116 | lifeskim:mentions | umls-concept:C0443331 | lld:lifeskim |
| pubmed-article:18613116 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:18613116 | pubmed:dateCreated | 2008-7-21 | lld:pubmed |
| pubmed-article:18613116 | pubmed:abstractText | Transient elevations in Ca2+ have previously been shown to promote focal adhesion disassembly and cell motility through an unknown mechanism. In this study, evidence is provided to show that CaMK-II, a Ca2+/calmodulin dependent protein kinase, influences fibroblast adhesion and motility. TIRF microscopy reveals a dynamic population of CaMK-II at the cell surface in migrating cells. Inhibition of CaMK-II with two mechanistically distinct, membrane permeant inhibitors (KN-93 and myr-AIP) freezes lamellipodial dynamics, accelerates spreading on fibronectin, enlarges paxillin-containing focal adhesions and blocks cell motility. In contrast, constitutively active CaMK-II is not found at the cell surface, reduces cell attachment, eliminates paxillin from focal adhesions and decreases the phospho-tyrosine levels of both FAK and paxillin; all of these events can be reversed with myr-AIP. Thus, both CaMK-II inhibition and constitutive activation block cell motility through over-stabilization or destabilization of focal adhesions, respectively. Coupled with the existence of transient Ca2+ elevations and a dynamic CaMK-II population, these findings provide the first direct evidence that CaMK-II enables cell motility by transiently and locally stimulating tyrosine dephosphorylation of focal adhesion proteins to promote focal adhesion turnover. | lld:pubmed |
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| pubmed-article:18613116 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18613116 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18613116 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18613116 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18613116 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18613116 | pubmed:month | Aug | lld:pubmed |
