Group:MUZIC:XIN: Difference between revisions

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== Interactions with other proteins/Function Function == | == Interactions with other proteins/Function Function == | ||
Xin and Mena/VASP colocalize with filamin c in [intercalated discs][http://en.wikipedia.org/wiki/Intercalated_disc](ICD, structure at the end of the myocytes that transduce force from the myofibrils via the cell membranes to the extracelluar matrix and neighboring cells) | Xin and Mena/VASP colocalize with filamin c in [intercalated discs][http://en.wikipedia.org/wiki/Intercalated_disc](ICD, structure at the end of the myocytes that transduce force from the myofibrils via the cell membranes to the extracelluar matrix and neighboring cells) in the adult heart <ref>PMID:19773341</ref>. | ||
Xin directly binds the EVH1 domain proteins Mena and VASP <ref name="pmid16631741">. | Xin directly binds the EVH1 domain proteins Mena and VASP <ref name="pmid16631741">. | ||
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== References == | == References == |
Revision as of 02:57, 12 July 2011
Xin actin-binding repeat-containing protein 1 (Alternative name: Cardiomyopathy-associated protein 1) is coded by the gene (Synonyms:CMYA1, XIN) and has an actin-binding domain (ABD). It crosslinks actin filaments and participates in anchoring of membrane proteins. Intraexogic splicing leads to a least three different isoforms.
Sequence AnnotationSequence Annotation
Interactions with other proteins/Function FunctionInteractions with other proteins/Function Function
Xin and Mena/VASP colocalize with filamin c in [intercalated discs][1](ICD, structure at the end of the myocytes that transduce force from the myofibrils via the cell membranes to the extracelluar matrix and neighboring cells) in the adult heart [1].
Xin directly binds the EVH1 domain proteins Mena and VASP <ref name="pmid16631741">. Xin binds the unique insertion containing Ig domain 20. Xin directly binds F-actin <ref name="pmid15454575">.
ReferencesReferences
ReferencesReferences
- ↑ Clark AR, Sawyer GM, Robertson SP, Sutherland-Smith AJ. Skeletal dysplasias due to filamin A mutations result from a gain-of-function mechanism distinct from allelic neurological disorders. Hum Mol Genet. 2009 Dec 15;18(24):4791-800. Epub 2009 Sep 22. PMID:19773341 doi:10.1093/hmg/ddp442