| pubmed-article:15492270 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15492270 | lifeskim:mentions | umls-concept:C0286983 | lld:lifeskim |
| pubmed-article:15492270 | lifeskim:mentions | umls-concept:C1705784 | lld:lifeskim |
| pubmed-article:15492270 | lifeskim:mentions | umls-concept:C0027627 | lld:lifeskim |
| pubmed-article:15492270 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:15492270 | lifeskim:mentions | umls-concept:C0812444 | lld:lifeskim |
| pubmed-article:15492270 | lifeskim:mentions | umls-concept:C0598435 | lld:lifeskim |
| pubmed-article:15492270 | lifeskim:mentions | umls-concept:C2003905 | lld:lifeskim |
| pubmed-article:15492270 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:15492270 | pubmed:dateCreated | 2004-10-19 | lld:pubmed |
| pubmed-article:15492270 | pubmed:abstractText | The cancer metastasis suppressor protein KAI1/CD82 is a member of the tetraspanin superfamily. Recent studies have demonstrated that tetraspanins are palmitoylated and that palmitoylation contributes to the organization of tetraspanin webs or tetraspanin-enriched microdomains. However, the effect of palmitoylation on tetraspanin-mediated cellular functions remains obscure. In this study, we found that tetraspanin KAI1/CD82 was palmitoylated when expressed in PC3 metastatic prostate cancer cells and that palmitoylation involved all of the cytoplasmic cysteine residues proximal to the plasma membrane. Notably, the palmitoylation-deficient KAI1/CD82 mutant largely reversed the wild-type KAI1/CD82's inhibitory effects on migration and invasion of PC3 cells. Also, palmitoylation regulates the subcellular distribution of KAI1/CD82 and its association with other tetraspanins, suggesting that the localized interaction of KAI1/CD82 with tetraspanin webs or tetraspanin-enriched microdomains is important for KAI1/CD82's motility-inhibitory activity. Moreover, we found that KAI1/CD82 palmitoylation affected motility-related subcellular events such as lamellipodia formation and actin cytoskeleton organization and that the alteration of these processes likely contributes to KAI1/CD82's inhibition of motility. Finally, the reversal of cell motility seen in the palmitoylation-deficient KAI1/CD82 mutant correlates with regaining of p130(CAS)-CrkII coupling, a signaling step important for KAI1/CD82's activity. Taken together, our results indicate that palmitoylation is crucial for the functional integrity of tetraspanin KAI1/CD82 during the suppression of cancer cell migration and invasion. | lld:pubmed |
| pubmed-article:15492270 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15492270 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15492270 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15492270 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15492270 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:15492270 | pubmed:issn | 0008-5472 | lld:pubmed |
| pubmed-article:15492270 | pubmed:author | pubmed-author:JosKK | lld:pubmed |
| pubmed-article:15492270 | pubmed:author | pubmed-author:ZhouBinB | lld:pubmed |
| pubmed-article:15492270 | pubmed:author | pubmed-author:ZhangXin AXA | lld:pubmed |
| pubmed-article:15492270 | pubmed:author | pubmed-author:ReddivariMura... | lld:pubmed |
| pubmed-article:15492270 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15492270 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:15492270 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:15492270 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15492270 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15492270 | pubmed:pagination | 7455-63 | lld:pubmed |
| pubmed-article:15492270 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:15492270 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15492270 | pubmed:articleTitle | The palmitoylation of metastasis suppressor KAI1/CD82 is important for its motility- and invasiveness-inhibitory activity. | lld:pubmed |
| pubmed-article:15492270 | pubmed:affiliation | Vascular Biology Center and Department of Medicine and Department of Molecular Science, University of Tennessee Health Science Center, Memphis, Tennessee, USA. | lld:pubmed |
| pubmed-article:15492270 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15492270 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15492270 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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