Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1 Journal Article
| Authors: | Howard, L.; Nelson, K. K.; Maciewicz, R. A.; Blobel, C. P. |
| Article Title: | Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1 |
| Abstract: | Metalloprotease disintegrins (a disintegrin and metalloprotease (ADAM) and metalloprotease, disintegrin, cysteine-rich proteins (MDC)) are a family of membrane-anchored glycoproteins that function in diverse biological processes, including fertilization, neurogenesis, myogenesis, and ectodomain processing of cytokines and other proteins. The cytoplasmic domains of ADAMs often include putative signaling motifs, such as proline-rich SH3 ligand domains, suggesting that interactions with cytoplasmic proteins may affect metalloprotease disintegrin function. Here we report that two SH3 domain- containing proteins, endophilin I (SH3GL2, SH3p4) and a novel SH3 domain- and phox homology (PX) domain-containing protein, termed SH3PX1, can interact with the cytoplasmic domains of the metalloprotease disintegrins MDC9 and MDC15. These interactions were initially identified in a yeast two-hybrid screen and then confirmed using bacterial fusion proteins and co- immunoprecipitations from eukaryotic cells expressing both binding partners. SH3PX1 and endophilin I both preferentially bind the precursor but not the processed form of MDC9 and MDC15 in COS-7 cells. Since rat endophilin I is thought to play a role in synaptic vesicle endocytosis and SH3PX1 has sequence similarity to sorting nexins in yeast, we propose that endophilin I and SH3PX1 may have a role in regulating the function of MDC9 and MDC15 by influencing their intracellular processing, transport, or final subcellular localization. |
| Keywords: | controlled study; sequence analysis; protein domain; protein localization; animals; mice; cell protein; protein binding; membrane proteins; protein interaction; cos cells; molecular cloning; cloning, molecular; protein processing; amino acid sequence; molecular sequence data; protein processing, post-translational; recombinant fusion proteins; nucleotide sequence; carrier proteins; protein transport; immunoprecipitation; adaptor proteins, signal transducing; cellular distribution; cytoplasm; dna sequence; yeast; glycoprotein; integrin; metalloproteinase; adam proteins; proline; receptors, cell surface; sequence analysis, dna; two-hybrid system techniques; protein precursors; vesicular transport proteins; amyloid beta-protein precursor; eukaryotic cells; disintegrins; metalloendopeptidases; humans; priority journal; article; cell compartmentation; src homology domains |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 274 |
| Issue: | 44 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 1999-10-29 |
| Start Page: | 31693 |
| End Page: | 31699 |
| Language: | English |
| DOI: | 10.1074/jbc.274.44.31693 |
| PUBMED: | 10531379 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |
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