Biology:APBA2
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Amyloid beta A4 precursor protein-binding family A member 2 is a protein that in humans is encoded by the APBA2 gene.[1][2]
Structure
This protein has phosphotyrosine-binding domain (PTB domain or PID) in the middle and two PDZ domains at C-terminal.
Function
The protein encoded by this gene is a member of the X11 protein family. It is a neuronal adaptor protein that interacts with the Alzheimer's disease amyloid precursor protein (APP). It stabilises APP and inhibits production of proteolytic APP fragments including the A beta peptide that is deposited in the brains of Alzheimer's disease patients. This gene product is believed to be involved in signal transduction processes. It is also regarded as a putative vesicular trafficking protein in the brain that can form a complex with the potential to couple synaptic vesicle exocytosis to neuronal cell adhesion.[2]
Interactions
APBA2 has been shown to interact with CLSTN1,[3][4] RELA[5] and amyloid precursor protein.[3][6][7]
References
- ↑ "The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system". FEBS Lett 397 (2–3): 197–200. January 1997. doi:10.1016/S0014-5793(96)01128-3. PMID 8955346.
- ↑ 2.0 2.1 "Entrez Gene: APBA2 amyloid beta (A4) precursor protein-binding, family A, member 2 (X11-like)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=321.
- ↑ 3.0 3.1 "Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism". J. Biol. Chem. 278 (49): 49448–58. December 2003. doi:10.1074/jbc.M306024200. PMID 12972431.
- ↑ "Coordinated metabolism of Alcadein and amyloid beta-protein precursor regulates FE65-dependent gene transactivation". J. Biol. Chem. 279 (23): 24343–54. June 2004. doi:10.1074/jbc.M401925200. PMID 15037614.
- ↑ "PDZ domain-dependent suppression of NF-kappaB/p65-induced Abeta42 production by a neuron-specific X11-like protein". J. Biol. Chem. 275 (17): 13056–60. April 2000. doi:10.1074/jbc.C000019200. PMID 10777610.
- ↑ "Regulation of APP-dependent transcription complexes by Mint/X11s: differential functions of Mint isoforms". J. Neurosci. 22 (17): 7340–51. September 2002. doi:10.1523/JNEUROSCI.22-17-07340.2002. PMID 12196555.
- ↑ "Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein". J. Biol. Chem. 274 (4): 2243–54. January 1999. doi:10.1074/jbc.274.4.2243. PMID 9890987.
External links
- Human APBA2 genome location and APBA2 gene details page in the UCSC Genome Browser.
Further reading
- "The PTB domain: a new protein module implicated in signal transduction". Trends Biochem. Sci. 20 (7): 277–80. 1995. doi:10.1016/S0968-0004(00)89043-X. PMID 7545337.
- "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. 1996. doi:10.1006/abio.1996.0138. PMID 8619474.
- "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. 1997. doi:10.1101/gr.7.4.353. PMID 9110174.
- "Mints, Munc18-interacting proteins in synaptic vesicle exocytosis". J. Biol. Chem. 272 (50): 31459–64. 1998. doi:10.1074/jbc.272.50.31459. PMID 9395480.
- "Mapping of the human and murine X11-like genes (APBA2 and apba2), the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2): genes encoding phosphotyrosine-binding domain proteins that interact with the Alzheimer's disease amyloid precursor protein". Mamm. Genome 9 (6): 473–5. 1998. doi:10.1007/s003359900800. PMID 9585438.
- "The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion". J. Biol. Chem. 273 (24): 14761–6. 1998. doi:10.1074/jbc.273.24.14761. PMID 9614075.
- "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 (48): 31633–6. 1998. doi:10.1074/jbc.273.48.31633. PMID 9822620.
- "Mint 3: a ubiquitous mint isoform that does not bind to munc18-1 or -2". Eur. J. Cell Biol. 77 (3): 161–5. 1999. doi:10.1016/s0171-9335(98)80103-9. PMID 9860131.
- "Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein". J. Biol. Chem. 274 (4): 2243–54. 1999. doi:10.1074/jbc.274.4.2243. PMID 9890987.
- "Mint2/X11-like colocalizes with the Alzheimer's disease amyloid precursor protein and is associated with neuritic plaques in Alzheimer's disease". Eur. J. Neurosci. 11 (6): 1988–94. 1999. doi:10.1046/j.1460-9568.1999.00610.x. PMID 10336668.
- "PDZ domain-dependent suppression of NF-kappaB/p65-induced Abeta42 production by a neuron-specific X11-like protein". J. Biol. Chem. 275 (17): 13056–60. 2000. doi:10.1074/jbc.C000019200. PMID 10777610.
- "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". J. Biol. Chem. 275 (33): 25616–24. 2000. doi:10.1074/jbc.M000955200. PMID 10827173.
- "Regulation of X11L-dependent amyloid precursor protein metabolism by XB51, a novel X11L-binding protein". J. Biol. Chem. 275 (30): 23134–8. 2000. doi:10.1074/jbc.C000302200. PMID 10833507.
- "Mints as adaptors. Direct binding to neurexins and recruitment of munc18". J. Biol. Chem. 275 (51): 39803–6. 2001. doi:10.1074/jbc.C000656200. PMID 11036064.
- "X11 alpha and x11 beta interact with presenilin-1 via their PDZ domains". Mol. Cell. Neurosci. 16 (5): 557–65. 2001. doi:10.1006/mcne.2000.0898. PMID 11083918.
- "Partial duplication of the APBA2 gene in chromosome 15q13 corresponds to duplicon structures". BMC Genomics 4 (1): 15. 2003. doi:10.1186/1471-2164-4-15. PMID 12720574.
- "XB51 isoforms mediate Alzheimer's beta-amyloid peptide production by X11L (X11-like protein)-dependent and -independent mechanisms". Biochem. J. 374 (Pt 1): 261–8. 2003. doi:10.1042/BJ20030489. PMID 12780348.
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