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Actinin-associated LIM Protein: Identification of a Domain Interaction between PDZ and Spectrin-like Repeat Motifs
| Content Provider | Scilit |
|---|---|
| Author | Xia, Houhui Winokur, Sara T. Kuo, Wen-Lin Altherr, Michael R. Bredt, David S. |
| Copyright Year | 1997 |
| Description | PDZ motifs are protein–protein interaction domains that often bind to COOH-terminal peptide sequences. The two PDZ proteins characterized in skeletal muscle, syntrophin and neuronal nitric oxide synthase, occur in the dystrophin complex, suggesting a role for PDZ proteins in muscular dystrophy. Here, we identify actinin-associated LIM protein (ALP), a novel protein in skeletal muscle that contains an NH2-terminal PDZ domain and a COOH-terminal LIM motif. ALP is expressed at high levels only in differentiated skeletal muscle, while an alternatively spliced form occurs at low levels in the heart. ALP is not a component of the dystrophin complex, but occurs in association with α-actinin-2 at the Z lines of myofibers. Biochemical and yeast two-hybrid analyses demonstrate that the PDZ domain of ALP binds to the spectrin-like motifs of α-actinin-2, defining a new mode for PDZ domain interactions. Fine genetic mapping studies demonstrate that ALP occurs on chromosome 4q35, near the heterochromatic locus that is mutated in fascioscapulohumeral muscular dystrophy. |
| Related Links | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139795/pdf http://jcb.rupress.org/content/jcb/139/2/507.full.pdf |
| Ending Page | 515 |
| Page Count | 9 |
| Starting Page | 507 |
| DOI | 10.1083/jcb.139.2.507 |
| Journal | Journal of Cell Biology |
| Issue Number | 2 |
| Volume Number | 139 |
| Language | English |
| Publisher | Rockefeller University Press |
| Publisher Date | 1997-10-20 |
| Access Restriction | Open |
| Subject Keyword | Cell Biology Protein Pdz Domain Alp Motifs Differentiated Binds Actinin Spectrin Like Journal: Journal of Cell Biology (Vol- 139, Issue- 2) |
| Content Type | Text |