APBA2
Amyloid beta A4 precursor protein-binding family A member 2 is a protein that in humans is encoded by the APBA2 gene.[1][2]
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
- ^ McLoughlin DM, Miller CC (Jan 1997). "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. doi:10.1016/S0014-5793(96)01128-3. PMID 8955346.
- ^ a b "Entrez Gene: APBA2 amyloid beta (A4) precursor protein-binding, family A, member 2 (X11-like)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=321.
- ^ a b Araki, Yoichi; Tomita Susumu, Yamaguchi Haruyasu, Miyagi Naomi, Sumioka Akio, Kirino Yutaka, Suzuki Toshiharu (Dec. 2003). "Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism". J. Biol. Chem. (United States) 278 (49): 49448–58. doi:10.1074/jbc.M306024200. ISSN 0021-9258. PMID 12972431.
- ^ Araki, Yoichi; Miyagi Naomi, Kato Naoko, Yoshida Tomohiro, Wada Sachiyo, Nishimura Masaki, Komano Hiroto, Yamamoto Tohru, De Strooper Bart, Yamamoto Kazuo, Suzuki Toshiharu (Jun. 2004). "Coordinated metabolism of Alcadein and amyloid beta-protein precursor regulates FE65-dependent gene transactivation". J. Biol. Chem. (United States) 279 (23): 24343–54. doi:10.1074/jbc.M401925200. ISSN 0021-9258. PMID 15037614.
- ^ Tomita, S; Fujita T, Kirino Y, Suzuki T (Apr. 2000). "PDZ domain-dependent suppression of NF-kappaB/p65-induced Abeta42 production by a neuron-specific X11-like protein". J. Biol. Chem. (UNITED STATES) 275 (17): 13056–60. doi:10.1074/jbc.C000019200. ISSN 0021-9258. PMID 10777610.
- ^ Biederer, Thomas; Cao Xinwei, Südhof Thomas C, Liu Xinran (Sep. 2002). "Regulation of APP-dependent transcription complexes by Mint/X11s: differential functions of Mint isoforms". J. Neurosci. (United States) 22 (17): 7340–51. PMID 12196555.
- ^ Tomita, S; Ozaki T, Taru H, Oguchi S, Takeda S, Yagi Y, Sakiyama S, Kirino Y, Suzuki T (Jan. 1999). "Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein". J. Biol. Chem. (UNITED STATES) 274 (4): 2243–54. doi:10.1074/jbc.274.4.2243. ISSN 0021-9258. PMID 9890987.
Further reading
- van der Geer P, Pawson T (1995). "The PTB domain: a new protein module implicated in signal transduction". Trends Biochem. Sci. 20 (7): 277–80. doi:10.1016/S0968-0004(00)89043-X. PMID 7545337.
- Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
- Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139146.
- Okamoto M, Südhof TC (1998). "Mints, Munc18-interacting proteins in synaptic vesicle exocytosis". J. Biol. Chem. 272 (50): 31459–64. doi:10.1074/jbc.272.50.31459. PMID 9395480.
- Blanco G, Irving NG, Brown SD, et al. (1998). "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. doi:10.1007/s003359900800. PMID 9585438.
- Borg JP, Yang Y, De Taddéo-Borg M, et al. (1998). "The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion". J. Biol. Chem. 273 (24): 14761–6. doi:10.1074/jbc.273.24.14761. PMID 9614075.
- Borg JP, Straight SW, Kaech SM, et al. (1998). "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 (48): 31633–6. doi:10.1074/jbc.273.48.31633. PMID 9822620.
- Okamoto M, Südhof TC (1999). "Mint 3: a ubiquitous mint isoform that does not bind to munc18-1 or -2". Eur. J. Cell Biol. 77 (3): 161–5. PMID 9860131.
- Tomita S, Ozaki T, Taru H, et al. (1999). "Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein". J. Biol. Chem. 274 (4): 2243–54. doi:10.1074/jbc.274.4.2243. PMID 9890987.
- McLoughlin DM, Irving NG, Brownlees J, et al. (1999). "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. doi:10.1046/j.1460-9568.1999.00610.x. PMID 10336668.
- Tomita S, Fujita T, Kirino Y, Suzuki T (2000). "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. doi:10.1074/jbc.C000019200. PMID 10777610.
- Gotthardt M, Trommsdorff M, Nevitt MF, et al. (2000). "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. doi:10.1074/jbc.M000955200. PMID 10827173.
- Lee DS, Tomita S, Kirino Y, Suzuki T (2000). "Regulation of X11L-dependent amyloid precursor protein metabolism by XB51, a novel X11L-binding protein". J. Biol. Chem. 275 (30): 23134–8. doi:10.1074/jbc.C000302200. PMID 10833507.
- Biederer T, Südhof TC (2001). "Mints as adaptors. Direct binding to neurexins and recruitment of munc18". J. Biol. Chem. 275 (51): 39803–6. doi:10.1074/jbc.C000656200. PMID 11036064.
- Lau KF, McLoughlin DM, Standen C, Miller CC (2001). "X11 alpha and x11 beta interact with presenilin-1 via their PDZ domains". Mol. Cell. Neurosci. 16 (5): 557–65. doi:10.1006/mcne.2000.0898. PMID 11083918.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Sutcliffe JS, Han MK, Amin T, et al. (2003). "Partial duplication of the APBA2 gene in chromosome 15q13 corresponds to duplicon structures". BMC Genomics 4: 15. doi:10.1186/1471-2164-4-15. PMC 156605. PMID 12720574. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=156605.
- Sumioka A, Imoto S, Martins RN, et al. (2003). "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. doi:10.1042/BJ20030489. PMC 1223589. PMID 12780348. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1223589.
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PDB gallery
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1u39: Auto-inhibition Mechanism of X11s/Mints Family Scaffold Proteins Revealed by the Closed Conformation of the Tandem PDZ Domains
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1y7n: Solution structure of the second PDZ domain of the human neuronal adaptor X11alpha
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