ADP-ribosylation factor GTPase-activating protein 1 is an enzyme that in humans is encoded by the ARFGAP1 gene.[5][6] Two transcript variants encoding different isoforms have been found for this gene.

ARFGAP1
Protein ARFGAP1 PDB 3DWD.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesARFGAP1, ARF1GAP, HRIHFB2281, ADP ribosylation factor GTPase activating protein 1
External IDsOMIM: 608377 MGI: 2183559 HomoloGene: 5517 GeneCards: ARFGAP1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001281482
NM_001281483
NM_001281484
NM_018209
NM_175609

RefSeq (protein)

NP_001268411
NP_001268412
NP_001268413
NP_060679
NP_783202

Location (UCSC)Chr 20: 63.27 – 63.29 MbChr 2: 180.61 – 180.62 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

FunctionEdit

The protein encoded by this gene is a GTPase-activating protein (GAP) which associates with the Golgi apparatus and which interacts with ADP-ribosylation factor 1 (ARF1). The encoded protein promotes hydrolysis of ARF1-bound GTP and is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. The activity of this protein is stimulated by phosphoinositides and inhibited by phosphatidylcholine.[6]

The protein has two amphipathic lipid packing sensor motifs (ALPS), that let the protein sense the curvature of the membrane (<30 nm) or lipid packing defects, and in this way evaluate if the vesicle is mature and ready for coat disassembly.[7][8]

InteractionsEdit

ARFGAP1 has been shown to interact with KDELR1 and LRRK2.[9][10][11]

ReferencesEdit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101199 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027575 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Huber I, Rotman M, Pick E, Makler V, Rothem L, Cukierman E, Cassel D (February 2001). "Expression, purification, and properties of ADP-ribosylation factor (ARF) GTPase activating protein-1". Methods in Enzymology. 329: 307–16. doi:10.1016/S0076-6879(01)29092-2. PMID 11210549.
  6. ^ a b "Entrez Gene: ARFGAP1 ADP-ribosylation factor GTPase activating protein 1".
  7. ^ Mesmin B, Drin G, Levi S, Rawet M, Cassel D, Bigay J, Antonny B (February 2007). "Two lipid-packing sensor motifs contribute to the sensitivity of ArfGAP1 to membrane curvature". Biochemistry. 46 (7): 1779–90. doi:10.1021/bi062288w. PMID 17253781.
  8. ^ Antonny B (June 2011). "Mechanisms of membrane curvature sensing". Annual Review of Biochemistry. 80: 101–23. doi:10.1146/annurev-biochem-052809-155121. PMID 21438688.
  9. ^ Aoe T, Cukierman E, Lee A, Cassel D, Peters PJ, Hsu VW (December 1997). "The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a GTPase-activating protein for ARF1". The EMBO Journal. 16 (24): 7305–16. doi:10.1093/emboj/16.24.7305. PMC 1170331. PMID 9405360.
  10. ^ Majoul I, Straub M, Hell SW, Duden R, Söling HD (July 2001). "KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: measurements in living cells using FRET". Developmental Cell. 1 (1): 139–53. doi:10.1016/S1534-5807(01)00004-1. PMID 11703931.
  11. ^ Stafa K, Trancikova A, Webber PJ, Glauser L, West AB, Moore DJ (February 2012). "GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1". PLOS Genetics. 8 (2): e1002526. doi:10.1371/journal.pgen.1002526. PMC 3280333. PMID 22363216.

External linksEdit

Further readingEdit