Group:MUZIC:ZASP
From Proteopedia
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doi: 10.1083/jcb.146.2.465 | doi: 10.1083/jcb.146.2.465 | ||
http://jcb.rupress.org/content/146/2/465.full | http://jcb.rupress.org/content/146/2/465.full | ||
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| + | '''''ZASP''''' ('''Z'''-disk '''A'''lternatively '''S'''pliced '''P'''DZ domain protein), also referred to as LIM domain-binding protein 3 (LDB-3), is the 78 kDa, 727-amino-acid human ortholog of cypher, independently identified in heart and skeletal | ||
| + | muscle<ref>PMID:10427098</ref>. Five alternatively spliced isoforms of ZASP have been identified (UniProtKB: O75112)[http://www.uniprot.org/uniprot/O75112#section_features)]. Apart from the PDZ domain, ZASP possess an internal motif (ZASP-like motif) which confers the ability to interact with the spectrin repeats of α-actinin-2 <ref>doi:10.1016/j.yexcr.2005.12.036</ref>. | ||
=='''Sequence annotation and domain topology'''== | =='''Sequence annotation and domain topology'''== | ||
Revision as of 17:55, 8 July 2011
Contents |
Introduction
ZASP is a component protein of the striated muscle Z-disk and a member of the enigma family of proteins. Like most enigma family members, it possess an N-terminal PDZ domain and three C-terminal LIM domains. The structure of the N-terminal PDZ domain has been solved (PDB ID: 1RGW) The PDZ domain has recently been characterized to bind a very C-terminal class III motif in myotilin [1] and myozenin, two other Z-disk members prominent during myofibrillogenesis and sarcomerogenesis [[2]]. doi: 10.1083/jcb.146.2.465 http://jcb.rupress.org/content/146/2/465.full
ZASP (Z-disk Alternatively Spliced PDZ domain protein), also referred to as LIM domain-binding protein 3 (LDB-3), is the 78 kDa, 727-amino-acid human ortholog of cypher, independently identified in heart and skeletal muscle[1]. Five alternatively spliced isoforms of ZASP have been identified (UniProtKB: O75112)[3]. Apart from the PDZ domain, ZASP possess an internal motif (ZASP-like motif) which confers the ability to interact with the spectrin repeats of α-actinin-2 [2].
Sequence annotation and domain topology
Canonical PDZ domains are known to target proteins to sites of complex formation, as such ZASP has been suggested as the oracle of Z-disk multi-protein complexes. This is also supported by the fact that the PDZ domain interacts with alpha-actinin-2, myotiin, myozenin.... Image:ZASP.png
Structure
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Function and Interactions
Mutations within the c-terminal of ZASP has been identified....
Pathology
References
- ↑ Faulkner G, Pallavicini A, Formentin E, Comelli A, Ievolella C, Trevisan S, Bortoletto G, Scannapieco P, Salamon M, Mouly V, Valle G, Lanfranchi G. ZASP: a new Z-band alternatively spliced PDZ-motif protein. J Cell Biol. 1999 Jul 26;146(2):465-75. PMID:10427098
- ↑ Klaavuniemi T, Ylanne J. Zasp/Cypher internal ZM-motif containing fragments are sufficient to co-localize with alpha-actinin--analysis of patient mutations. Exp Cell Res. 2006 May 1;312(8):1299-311. Epub 2006 Feb 14. PMID:16476425 doi:10.1016/j.yexcr.2005.12.036
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