Biology:VAP protein family
From HandWiki
| VAMP-associated membrane protein | |
|---|---|
| Identifiers | |
| Symbol | VAP |
| InterPro | IPR016763 |
| Membranome | 202 |
VAP proteins are conserved integral membrane proteins of the endoplasmic reticulum found in all eukaryotic cells.[1] VAP stands for VAMP-associated protein,[2] where VAMP stands for vesicle-associated membrane protein. Humans have two VAPs that consist of the essential Major Sperm Protein domain and linker plus transmembrane helix) to attach to the ER: VAPA and VAPB.[3] A third VAP-like protein is Motile sperm domain containing 2 (MOSPD2), which has all the elements of VAP, and like them binds FFAT motifs, but has at its N-terminus a CRAL-TRIO domain that can bind and transfer lipids.[4]
VAP includes the whole family of protein homologues in all species. For example, baker's yeast expresses two VAPs: Scs2 and Scs22.[5][6]
References
- ↑ "Identification of a human homologue of the vesicle-associated membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a broadly expressed protein that binds to VAMP". The Biochemical Journal 333 (2): 247–51. July 1998. doi:10.1042/bj3330247. PMID 9657962.
- ↑ "A VAMP-binding protein from Aplysia required for neurotransmitter release". Science 269 (5230): 1580–3. September 1995. doi:10.1126/science.7667638. PMID 7667638. Bibcode: 1995Sci...269.1580S.
- ↑ "Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins". Biochemical and Biophysical Research Communications 254 (1): 21–6. January 1999. doi:10.1006/bbrc.1998.9876. PMID 9920726.
- ↑ Di Mattia, Thomas; Wilhelm, Léa P.; Ikhlef, Souade; Wendling, Corinne; Spehner, Danièle; Nominé, Yves; Giordano, Francesca; Mathelin, Carole et al. (July 2018). "Identification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites". EMBO Reports 19 (7). doi:10.15252/embr.201745453. ISSN 1469-3178. PMID 29858488.
- ↑ "Cloning and sequence of the SCS2 gene, which can suppress the defect of INO1 expression in an inositol auxotrophic mutant of Saccharomyces cerevisiae". Journal of Biochemistry 118 (1): 39–45. July 1995. doi:10.1093/oxfordjournals.jbchem.a124889. PMID 8537323.
- ↑ "A highly conserved binding site in vesicle-associated membrane protein-associated protein (VAP) for the FFAT motif of lipid-binding proteins". The Journal of Biological Chemistry 280 (14): 14097–104. April 2005. doi:10.1074/jbc.M500147200. PMID 15668246.
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