APBA1
Amyloid beta A4 precursor protein-binding family A member 1 is a protein that in humans is encoded by the APBA1 gene.[1][2][3]
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.[3]
Interactions
APBA1 has been shown to interact with KCNJ12,[4][5] CCS,[6] CASK[7][8] and Amyloid precursor protein.[9][10]
References
- ^ Duclos F, Boschert U, Sirugo G, Mandel JL, Hen R, Koenig M (Feb 1993). "Gene in the region of the Friedreich ataxia locus encodes a putative transmembrane protein expressed in the nervous system". Proc Natl Acad Sci U S A 90 (1): 109–13. doi:10.1073/pnas.90.1.109. PMC 45609. PMID 7678331. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=45609.
- ^ Duclos F, Koenig M (May 1995). "Comparison of primary structure of a neuron-specific protein, X11, between human and mouse". Mamm Genome 6 (1): 57–8. doi:10.1007/BF00350899. PMID 7719031.
- ^ a b "Entrez Gene: APBA1 amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=320.
- ^ Leonoudakis, Dmitri; Conti Lisa R, Anderson Scott, Radeke Carolyn M, McGuire Leah M M, Adams Marvin E, Froehner Stanley C, Yates John R, Vandenberg Carol A (May. 2004). "Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins". J. Biol. Chem. (United States) 279 (21): 22331–46. doi:10.1074/jbc.M400285200. ISSN 0021-9258. PMID 15024025.
- ^ Leonoudakis, Dmitri; Conti Lisa R, Radeke Carolyn M, McGuire Leah M M, Vandenberg Carol A (Apr. 2004). "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels". J. Biol. Chem. (United States) 279 (18): 19051–63. doi:10.1074/jbc.M400284200. ISSN 0021-9258. PMID 14960569.
- ^ McLoughlin, D M; Standen C L, Lau K F, Ackerley S, Bartnikas T P, Gitlin J D, Miller C C (Mar. 2001). "The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity". J. Biol. Chem. (United States) 276 (12): 9303–7. doi:10.1074/jbc.M010023200. ISSN 0021-9258. PMID 11115513.
- ^ Borg, J P; Straight S W, Kaech S M, de Taddéo-Borg M, Kroon D E, Karnak D, Turner R S, Kim S K, Margolis B (Nov. 1998). "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. (UNITED STATES) 273 (48): 31633–6. doi:10.1074/jbc.273.48.31633. ISSN 0021-9258. PMID 9822620.
- ^ Borg, J P; Lõpez-Figueroa M O, de Taddèo-Borg M, Kroon D E, Turner R S, Watson S J, Margolis B (Feb. 1999). "Molecular analysis of the X11-mLin-2/CASK complex in brain". J. Neurosci. (UNITED STATES) 19 (4): 1307–16. ISSN 0270-6474. PMID 9952408.
- ^ 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.
- ^ Borg, J P; Ooi J, Levy E, Margolis B (Nov. 1996). "The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein". Mol. Cell. Biol. (UNITED STATES) 16 (11): 6229–41. ISSN 0270-7306. PMC 231626. PMID 8887653. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231626.
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.
- Chen WJ, Goldstein JL, Brown MS (1990). "NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor.". J. Biol. Chem. 265 (6): 3116–23. PMID 1968060.
- Borg JP, Ooi J, Levy E, Margolis B (1996). "The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein.". Mol. Cell. Biol. 16 (11): 6229–41. PMC 231626. PMID 8887653. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231626.
- Zhang Z, Lee CH, Mandiyan V, et al. (1997). "Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain.". EMBO J. 16 (20): 6141–50. doi:10.1093/emboj/16.20.6141. PMC 1326298. PMID 9321393. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1326298.
- 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.
- Butz S, Okamoto M, Südhof TC (1998). "A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain.". Cell 94 (6): 773–82. doi:10.1016/S0092-8674(00)81736-5. PMID 9753324.
- 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.
- Borg JP, Lõpez-Figueroa MO, de Taddèo-Borg M, et al. (1999). "Molecular analysis of the X11-mLin-2/CASK complex in brain.". J. Neurosci. 19 (4): 1307–16. PMID 9952408.
- Maximov A, Südhof TC, Bezprozvanny I (1999). "Association of neuronal calcium channels with modular adaptor proteins.". J. Biol. Chem. 274 (35): 24453–6. doi:10.1074/jbc.274.35.24453. PMID 10455105.
- Mueller HT, Borg JP, Margolis B, Turner RS (2001). "Modulation of amyloid precursor protein metabolism by X11alpha /Mint-1. A deletion analysis of protein-protein interaction domains.". J. Biol. Chem. 275 (50): 39302–6. doi:10.1074/jbc.M008453200. PMID 11010978.
- 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.
- McLoughlin DM, Standen CL, Lau KF, et al. (2001). "The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity.". J. Biol. Chem. 276 (12): 9303–7. doi:10.1074/jbc.M010023200. PMID 11115513.
- Bécamel C, Alonso G, Galéotti N, et al. (2002). "Synaptic multiprotein complexes associated with 5-HT(2C) receptors: a proteomic approach.". EMBO J. 21 (10): 2332–42. doi:10.1093/emboj/21.10.2332. PMC 126011. PMID 12006486. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=126011.
- Ho CS, Marinescu V, Steinhilb ML, et al. (2002). "Synergistic effects of Munc18a and X11 proteins on amyloid precursor protein metabolism.". J. Biol. Chem. 277 (30): 27021–8. doi:10.1074/jbc.M201823200. PMID 12016213.
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PDB gallery
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1aqc: X11 PTB DOMAIN-10MER PEPTIDE COMPLEX
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1u37: Auto-inhibition Mechanism of X11s/Mints Family Scaffold Proteins Revealed by the Closed Conformation of the Tandem PDZ Domains
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1u38: Auto-inhibition Mechanism of X11s/Mints Family Scaffold Proteins Revealed by the Closed Conformation of the Tandem PDZ Domains
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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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1u3b: Auto-inhibition Mechanism of X11s/Mints Family Scaffold Proteins Revealed by the Closed Conformation of the Tandem PDZ Domains
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1x45: Solution structure of the first PDZ domain of amyloid beta A4 precursor protein-binding family A, member 1
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1y7n: Solution structure of the second PDZ domain of the human neuronal adaptor X11alpha
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