| pubmed-article:19047374 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19047374 | lifeskim:mentions | umls-concept:C0026848 | lld:lifeskim |
| pubmed-article:19047374 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:19047374 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:19047374 | lifeskim:mentions | umls-concept:C0230719 | lld:lifeskim |
| pubmed-article:19047374 | lifeskim:mentions | umls-concept:C1422182 | lld:lifeskim |
| pubmed-article:19047374 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:19047374 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:19047374 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:19047374 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
| pubmed-article:19047374 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
| pubmed-article:19047374 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:19047374 | lifeskim:mentions | umls-concept:C0205214 | lld:lifeskim |
| pubmed-article:19047374 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:19047374 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:19047374 | pubmed:dateCreated | 2009-1-19 | lld:pubmed |
| pubmed-article:19047374 | pubmed:abstractText | Interactions between Z-disc proteins regulate muscle functions and disruption of these interactions results in muscle disorders. Mutations in Z-disc components myotilin, ZASP/Cypher, and FATZ-2 (calsarcin-1/myozenin-2) are associated with myopathies. We report here that the myotilin and the FATZ (calsarcin/myozenin) families share high homology at their final C-terminal five amino acids. This C-terminal E[ST][DE][DE]L motif is present almost exclusively in these families and is evolutionary conserved. We show by in vitro and in vivo studies that proteins from the myotilin and FATZ (calsarcin/myozenin) families interact via this novel type of class III PDZ binding motif with the PDZ domains of ZASP/Cypher and other Enigma family members: ALP, CLP-36, and RIL. We show that the interactions can be modulated by phosphorylation. Calmodulin-dependent kinase II phosphorylates the C terminus of FATZ-3 (calsarcin-3/myozenin-3) and myotilin, whereas PKA phosphorylates that of FATZ-1 (calsarcin-2/myozenin-1) and FATZ-2 (calsarcin-1/myozenin-1). This is the first report of a binding motif common to both the myotilin and the FATZ (calsarcin/myozenin) families that is specific for interactions with Enigma family members. | lld:pubmed |
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| pubmed-article:19047374 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19047374 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19047374 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19047374 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19047374 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19047374 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:19047374 | pubmed:issn | 1098-5549 | lld:pubmed |
| pubmed-article:19047374 | pubmed:author | pubmed-author:ValleGiorgioG | lld:pubmed |
| pubmed-article:19047374 | pubmed:author | pubmed-author:FaulknerGeorg... | lld:pubmed |
| pubmed-article:19047374 | pubmed:author | pubmed-author:CarpenOlliO | lld:pubmed |
| pubmed-article:19047374 | pubmed:author | pubmed-author:SuilaHeliH | lld:pubmed |
| pubmed-article:19047374 | pubmed:author | pubmed-author:BelgranoAnnaA | lld:pubmed |
| pubmed-article:19047374 | pubmed:author | pubmed-author:ZaraIvanoI | lld:pubmed |
