APBA1

From Wikipedia, the free encyclopedia

Amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)

PDB rendering based on 1aqc.

Available structures: 1aqc, 1u37, 1u38, 1u39, 1u3b, 1x11, 1x45, 1y7n

Identifiers

Symbol(s)

APBA1; D9S411E; MINT1; X11; X11A; X11ALPHA

External IDs

OMIM: 602414 MGI: 1860297 HomoloGene: 897

Gene ontology
Molecular Function:	• protein binding
Cellular Component:	• synaptic vesicle
Biological Process:	• protein complex assembly • intracellular protein transport • cell adhesion • synaptic transmission • nervous system development • axon cargo transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_001163 (mRNA)
NP_001154 (protein)

NM_177034 (mRNA)
NP_796008 (protein)

Location

Chr 9: 71.24 - 71.48 Mb

Chr 19: 23.83 - 24.02 Mb

Pubmed search

[1]

[2]

Amyloid beta (A4) precursor protein-binding, family A, member 1 (X11), also known as APBA1, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: APBA1 amyloid beta (A4) precursor protein-binding, family A, member 1 (X11).

[edit] 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. 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.
Duclos F, Boschert U, Sirugo G, et al. (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. PMID 7678331.
Duclos F, Koenig M (1995). "Comparison of primary structure of a neuron-specific protein, X11, between human and mouse.". Mamm. Genome 6 (1): 57–8. PMID 7719031.
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. PMID 8887653.
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. PMID 9321393.
Okamoto M, Südhof TC (1998). "Mints, Munc18-interacting proteins in synaptic vesicle exocytosis.". J. Biol. Chem. 272 (50): 31459–64. 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. 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. 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. 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. 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. 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. PMID 12006486.
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.