| pubmed-article:9472040 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9472040 | lifeskim:mentions | umls-concept:C1317964 | lld:lifeskim |
| pubmed-article:9472040 | lifeskim:mentions | umls-concept:C0002520 | lld:lifeskim |
| pubmed-article:9472040 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:9472040 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
| pubmed-article:9472040 | lifeskim:mentions | umls-concept:C0059973 | lld:lifeskim |
| pubmed-article:9472040 | lifeskim:mentions | umls-concept:C1332712 | lld:lifeskim |
| pubmed-article:9472040 | lifeskim:mentions | umls-concept:C1414477 | lld:lifeskim |
| pubmed-article:9472040 | lifeskim:mentions | umls-concept:C0128818 | lld:lifeskim |
| pubmed-article:9472040 | lifeskim:mentions | umls-concept:C0139903 | lld:lifeskim |
| pubmed-article:9472040 | lifeskim:mentions | umls-concept:C1420364 | lld:lifeskim |
| pubmed-article:9472040 | lifeskim:mentions | umls-concept:C1704332 | lld:lifeskim |
| pubmed-article:9472040 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:9472040 | lifeskim:mentions | umls-concept:C1706211 | lld:lifeskim |
| pubmed-article:9472040 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9472040 | pubmed:dateCreated | 1998-3-16 | lld:pubmed |
| pubmed-article:9472040 | pubmed:abstractText | CD44 has been identified as a membrane-binding partner for ezrin/radixin/moesin (ERM) proteins, plasma membrane/actin filament cross-linkers. ERM proteins, however, are not necessarily colocalized with CD44 in tissues, but with CD43 and ICAM-2 in some types of cells. We found that glutathione-S-transferase fusion proteins with the cytoplasmic domain of CD43 and ICAM-2, as well as CD44, bound to moesin in vitro. The regions responsible for the in vitro binding of CD43 and CD44 to moesin were narrowed down to their juxta-membrane 20-30-amino acid sequences in the cytoplasmic domain. These sequences and the cytoplasmic domain of ICAM-2 (28 amino acids) were all characterized by the positively charged amino acid clusters. When E-cadherin chimeric molecules bearing these positively charged amino acid clusters of CD44, CD43, or ICAM-2 were expressed in mouse L fibroblasts, they were co-concentrated with ERM proteins at microvilli, whereas those lacking these clusters were diffusely distributed on the cell surface. The specific binding of ERM proteins to the juxta-membrane positively charged amino acid clusters of CD44, CD43, and ICAM-2 was confirmed by immunoprecipitation and site-directed mutagenesis. From these findings, we conclude that ERM proteins bind to integral membrane proteins bearing a positively charged amino acid cluster in their juxta-membrane cytoplasmic domain. | lld:pubmed |
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| pubmed-article:9472040 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9472040 | pubmed:citationSubset | IM | lld:pubmed |
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