ARFGAP1: Difference between revisions

Jump to navigation Jump to search
m (Bot: HTTP→HTTPS)
m (1 revision imported)
 
(One intermediate revision by one other user not shown)
Line 1: Line 1:
{{Infobox_gene}}
{{Infobox_gene}}
'''ADP-ribosylation factor GTPase-activating protein 1''' is an [[enzyme]] that in humans is encoded by the ''ARFGAP1'' [[gene]].<ref name="pmid11210549">{{cite journal | vauthors = Huber I, Rotman M, Pick E, Makler V, Rothem L, Cukierman E, Cassel D | title = Expression, purification, and properties of ADP-ribosylation factor (ARF) GTPase activating protein-1 | journal = Methods Enzymol | volume = 329 | issue =  | pages = 307–16 |date=February 2001 | pmid = 11210549 | pmc =  | doi =10.1016/S0076-6879(01)29092-2 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ARFGAP1 ADP-ribosylation factor GTPase activating protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55738| accessdate = }}</ref>  Two transcript variants encoding different isoforms have been found for this gene.
'''ADP-ribosylation factor GTPase-activating protein 1''' is an [[enzyme]] that in humans is encoded by the ''ARFGAP1'' [[gene]].<ref name="pmid11210549">{{cite journal | vauthors = Huber I, Rotman M, Pick E, Makler V, Rothem L, Cukierman E, Cassel D | title = Expression, purification, and properties of ADP-ribosylation factor (ARF) GTPase activating protein-1 | journal = Methods in Enzymology | volume = 329 | issue =  | pages = 307–16 | date = February 2001 | pmid = 11210549 | pmc =  | doi = 10.1016/S0076-6879(01)29092-2 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ARFGAP1 ADP-ribosylation factor GTPase activating protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55738| access-date = }}</ref>  Two transcript variants encoding different isoforms have been found for this gene.


== Function ==
== Function ==
Line 6: Line 6:
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 [[phosphoinositide]]s and inhibited by [[phosphatidylcholine]].<ref name="entrez"/>
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 [[phosphoinositide]]s and inhibited by [[phosphatidylcholine]].<ref name="entrez"/>


The protein has two [[amphipathic lipid packing sensor motifs]], that let the protein sense the curvature of the membrane (<30&nbsp;nm) or lipid packing defects, and in this way evaluate if the vesicule is mature and ready for coat disassembly.<ref name="pmid21438688">{{cite journal | author = Antonny, Bruno | title = Mechanisms of membrane curvature sensing | journal = Annu Rev Biochem | volume = 80 | issue =  | pages = 101–123 |date=June 2011 | pmid = 21438688 | pmc =  | doi =10.1146/annurev-biochem-052809-155121 }}</ref>
The protein has two [[amphipathic lipid packing sensor motifs]] (ALPS), that let the protein sense the curvature of the membrane (<30&nbsp;nm) or lipid packing defects, and in this way evaluate if the vesicle is mature and ready for coat disassembly.<ref>{{cite journal | vauthors = Mesmin B, Drin G, Levi S, Rawet M, Cassel D, Bigay J, Antonny B | title = Two lipid-packing sensor motifs contribute to the sensitivity of ArfGAP1 to membrane curvature | journal = Biochemistry | volume = 46 | issue = 7 | pages = 1779–90 | date = February 2007 | pmid = 17253781 | doi = 10.1021/bi062288w }}</ref><ref name="pmid21438688">{{cite journal | vauthors = Antonny B | title = Mechanisms of membrane curvature sensing | journal = Annual Review of Biochemistry | volume = 80 | issue =  | pages = 101–23 | date = June 2011 | pmid = 21438688 | pmc =  | doi = 10.1146/annurev-biochem-052809-155121 }}</ref>


==Interactions==
== Interactions ==


ARFGAP1 has been shown to [[Protein-protein interaction|interact]] with [[KDELR1]] and [[LRRK2]].<ref name="pmid9405360">{{cite journal | vauthors = Aoe T, Cukierman E, Lee A, Cassel D, Peters PJ, Hsu VW | title = The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a GTPase-activating protein for ARF1 | journal = EMBO J. | volume = 16 | issue = 24 | pages = 7305–16 |date=December 1997 | pmid = 9405360 | pmc = 1170331 | doi = 10.1093/emboj/16.24.7305 }}</ref><ref name="pmid11703931">{{cite journal | vauthors = Majoul I, Straub M, Hell SW, Duden R, Söling HD | title = KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: measurements in living cells using FRET | journal = Dev. Cell | volume = 1 | issue = 1 | pages = 139–53 |date=July 2001 | pmid = 11703931 | doi = 10.1016/S1534-5807(01)00004-1 }}</ref><ref name="pmid22363216">{{cite journal | vauthors = Stafa K, Trancikova A, Webber PJ, Glauser L, West AB, Moore DJ | title = GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1 | journal = PLoS Genet. | volume = 8 | issue = 2 | pages = e1002526 |date=February 2012 | pmid = 22363216 | pmc = 3280333 | doi = 10.1371/journal.pgen.1002526 | url = }}</ref>
ARFGAP1 has been shown to [[Protein-protein interaction|interact]] with [[KDELR1]] and [[LRRK2]].<ref name="pmid9405360">{{cite journal | vauthors = Aoe T, Cukierman E, Lee A, Cassel D, Peters PJ, Hsu VW | title = The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a GTPase-activating protein for ARF1 | journal = The EMBO Journal | volume = 16 | issue = 24 | pages = 7305–16 | date = December 1997 | pmid = 9405360 | pmc = 1170331 | doi = 10.1093/emboj/16.24.7305 }}</ref><ref name="pmid11703931">{{cite journal | vauthors = Majoul I, Straub M, Hell SW, Duden R, Söling HD | title = KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: measurements in living cells using FRET | journal = Developmental Cell | volume = 1 | issue = 1 | pages = 139–53 | date = July 2001 | pmid = 11703931 | doi = 10.1016/S1534-5807(01)00004-1 }}</ref><ref name="pmid22363216">{{cite journal | vauthors = Stafa K, Trancikova A, Webber PJ, Glauser L, West AB, Moore DJ | title = GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1 | journal = PLoS Genetics | volume = 8 | issue = 2 | pages = e1002526 | date = February 2012 | pmid = 22363216 | pmc = 3280333 | doi = 10.1371/journal.pgen.1002526 }}</ref>


==References==
== References ==
{{Reflist}}
{{Reflist}}
{{Clear}}
{{Clear}}


==External links==
== External links ==
* {{UCSC gene info|ARFGAP1}}
* {{UCSC gene info|ARFGAP1}}


==Further reading==
== Further reading ==
{{Refbegin | 2}}
{{Refbegin | 2}}
*{{cite journal | author=Rothman JE |title=Mechanisms of intracellular protein transport. |journal=Nature |volume=372 |issue= 6501 |pages= 55–63 |year= 1994 |pmid= 7969419 |doi= 10.1038/372055a0 }}
* {{cite journal | vauthors = Rothman JE | title = Mechanisms of intracellular protein transport | journal = Nature | volume = 372 | issue = 6501 | pages = 55–63 | date = November 1994 | pmid = 7969419 | doi = 10.1038/372055a0 }}
*{{cite journal | vauthors=Bernards A, Settleman J |title=GAP control: regulating the regulators of small GTPases. |journal=Trends Cell Biol. |volume=14 |issue= 7 |pages= 377–85 |year= 2005 |pmid= 15246431 |doi= 10.1016/j.tcb.2004.05.003 }}
* {{cite journal | vauthors = Bernards A, Settleman J | title = GAP control: regulating the regulators of small GTPases | journal = Trends in Cell Biology | volume = 14 | issue = 7 | pages = 377–85 | date = July 2004 | pmid = 15246431 | doi = 10.1016/j.tcb.2004.05.003 }}
*{{cite journal | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = January 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | vauthors=Cukierman E, Huber I, Rotman M, Cassel D |title=The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization |journal=Science |volume=270 |issue= 5244 |pages= 1999–2002 |year= 1996 |pmid= 8533093 |doi=10.1126/science.270.5244.1999 }}
* {{cite journal | vauthors = Cukierman E, Huber I, Rotman M, Cassel D | title = The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization | journal = Science | volume = 270 | issue = 5244 | pages = 1999–2002 | date = December 1995 | pmid = 8533093 | doi = 10.1126/science.270.5244.1999 }}
*{{cite journal | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 |display-authors=etal}}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = October 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | vauthors=Aoe T, Cukierman E, Lee A |title=The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a GTPase-activating protein for ARF1 |journal=EMBO J. |volume=16 |issue= 24 |pages= 7305–16 |year= 1998 |pmid= 9405360 |doi= 10.1093/emboj/16.24.7305 | pmc=1170331 |display-authors=etal}}
* {{cite journal | vauthors = Aoe T, Cukierman E, Lee A, Cassel D, Peters PJ, Hsu VW | title = The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a GTPase-activating protein for ARF1 | journal = The EMBO Journal | volume = 16 | issue = 24 | pages = 7305–16 | date = December 1997 | pmid = 9405360 | pmc = 1170331 | doi = 10.1093/emboj/16.24.7305 }}
*{{cite journal | vauthors=Mossessova E, Gulbis JM, Goldberg J |title=Structure of the guanine nucleotide exchange factor Sec7 domain of human arno and analysis of the interaction with ARF GTPase |journal=Cell |volume=92 |issue= 3 |pages= 415–23 |year= 1998 |pmid= 9476900 |doi=10.1016/S0092-8674(00)80933-2 }}
* {{cite journal | vauthors = Mossessova E, Gulbis JM, Goldberg J | title = Structure of the guanine nucleotide exchange factor Sec7 domain of human arno and analysis of the interaction with ARF GTPase | journal = Cell | volume = 92 | issue = 3 | pages = 415–23 | date = February 1998 | pmid = 9476900 | doi = 10.1016/S0092-8674(00)80933-2 }}
*{{cite journal | vauthors=Huber I, Cukierman E, Rotman M |title=Requirement for both the amino-terminal catalytic domain and a noncatalytic domain for in vivo activity of ADP-ribosylation factor GTPase-activating protein |journal=J. Biol. Chem. |volume=273 |issue= 38 |pages= 24786–91 |year= 1998 |pmid= 9733781 |doi=10.1074/jbc.273.38.24786 |display-authors=etal}}
* {{cite journal | vauthors = Huber I, Cukierman E, Rotman M, Aoe T, Hsu VW, Cassel D | title = Requirement for both the amino-terminal catalytic domain and a noncatalytic domain for in vivo activity of ADP-ribosylation factor GTPase-activating protein | journal = The Journal of Biological Chemistry | volume = 273 | issue = 38 | pages = 24786–91 | date = September 1998 | pmid = 9733781 | doi = 10.1074/jbc.273.38.24786 }}
*{{cite journal | vauthors=Zhang C, Yu Y, Zhang S |title=Characterization, chromosomal assignment, and tissue expression of a novel human gene belonging to the ARF GAP family |journal=Genomics |volume=63 |issue= 3 |pages= 400–8 |year= 2000 |pmid= 10704287 |doi= 10.1006/geno.1999.6095 |display-authors=etal}}
* {{cite journal | vauthors = Zhang C, Yu Y, Zhang S, Liu M, Xing G, Wei H, Bi J, Liu X, Zhou G, Dong C, Hu Z, Zhang Y, Luo L, Wu C, Zhao S, He F | title = Characterization, chromosomal assignment, and tissue expression of a novel human gene belonging to the ARF GAP family | journal = Genomics | volume = 63 | issue = 3 | pages = 400–8 | date = February 2000 | pmid = 10704287 | doi = 10.1006/geno.1999.6095 }}
*{{cite journal | vauthors=Majoul I, Straub M, Hell SW |title=KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: measurements in living cells using FRET |journal=Dev. Cell |volume=1 |issue= 1 |pages= 139–53 |year= 2001 |pmid= 11703931 |doi=10.1016/S1534-5807(01)00004-1 |display-authors=etal}}
* {{cite journal | vauthors = Majoul I, Straub M, Hell SW, Duden R, Söling HD | title = KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: measurements in living cells using FRET | journal = Developmental Cell | volume = 1 | issue = 1 | pages = 139–53 | date = July 2001 | pmid = 11703931 | doi = 10.1016/S1534-5807(01)00004-1 }}
*{{cite journal  | vauthors=Deloukas P, Matthews LH, Ashurst J |title=The DNA sequence and comparative analysis of human chromosome 20 |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a |display-authors=etal}}
* {{cite journal | vauthors = Yu S, Roth MG | title = Casein kinase I regulates membrane binding by ARF GAP1 | journal = Molecular Biology of the Cell | volume = 13 | issue = 8 | pages = 2559–70 | date = August 2002 | pmid = 12181329 | pmc = 117925 | doi = 10.1091/mbc.E02-04-0189 }}
*{{cite journal | vauthors=Yu S, Roth MG |title=Casein kinase I regulates membrane binding by ARF GAP1 |journal=Mol. Biol. Cell |volume=13 |issue= 8 |pages= 2559–70 |year= 2003 |pmid= 12181329 |doi= 10.1091/mbc.E02-04-0189 | pmc=117925 }}
* {{cite journal | vauthors = Yang JS, Lee SY, Gao M, Bourgoin S, Randazzo PA, Premont RT, Hsu VW | title = ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat | journal = The Journal of Cell Biology | volume = 159 | issue = 1 | pages = 69–78 | date = October 2002 | pmid = 12379802 | pmc = 2173491 | doi = 10.1083/jcb.200206015 }}
*{{cite journal | vauthors=Yang JS, Lee SY, Gao M |title=ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat |journal=J. Cell Biol. |volume=159 |issue= 1 |pages= 69–78 |year= 2002 |pmid= 12379802 |doi= 10.1083/jcb.200206015  | pmc=2173491 |display-authors=etal}}
* {{cite journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–5 | date = August 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
*{{cite journal | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | vauthors=Beausoleil SA, Jedrychowski M, Schwartz D |title=Large-scale characterization of HeLa cell nuclear phosphoproteins |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101  | pmc=514446 |display-authors=etal}}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
{{Refend}}
{{Refend}}


{{Gene-20-stub}}
{{Gene-20-stub}}

Latest revision as of 07:16, 10 January 2019

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

ADP-ribosylation factor GTPase-activating protein 1 is an enzyme that in humans is encoded by the ARFGAP1 gene.[1][2] Two transcript variants encoding different isoforms have been found for this gene.

Function

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.[2]

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.[3][4]

Interactions

ARFGAP1 has been shown to interact with KDELR1 and LRRK2.[5][6][7]

References

  1. 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.
  2. 2.0 2.1 "Entrez Gene: ARFGAP1 ADP-ribosylation factor GTPase activating protein 1".
  3. 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.
  4. 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.
  5. 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.
  6. 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.
  7. 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 links

Further reading