ARL2

ARL2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3DOE, 3DOF
Identifiers
Aliases	ARL2 , ARFL2, ADP ribosylation factor like GTPase 2, MRCS1
External IDs	OMIM: 601175 MGI: 1928393 HomoloGene: 1260 GeneCards: ARL2
Gene location (Human)
Chr.	Chromosome 11 (human)
End	65,022,184 bp
Gene location (Mouse)
Chr.	Chromosome 19 (mouse)
End	6,191,578 bp
RNA expression pattern
	Top expressed in
	nucleus accumbens; ; caudate nucleus; ; putamen; ; tibial nerve; ; left coronary artery; ; ascending aorta; ; popliteal artery; ; gastric mucosa; ; gastrocnemius muscle; ; right coronary artery;
	Top expressed in
	right ventricle; ; yolk sac; ; superior frontal gyrus; ; saccule; ; otic placode; ; facial motor nucleus; ; lens; ; ankle joint; ; cerebellar cortex; ; neural tube;
	More reference expression data
	n/a
Gene ontology
Molecular function	nucleotide binding ; GTP binding ; GTPase inhibitor activity ; protein binding ; GTPase activity ; GDP binding ;
Cellular component	cytoplasm ; centrosome ; lateral plasma membrane ; mitochondrial intermembrane space ; intracellular anatomical structure ; microtubule organizing center ; mitochondrial matrix ; mitochondrion ; cytoskeleton ; nucleus ; nucleolus ; Golgi apparatus ; cytosol ; focal adhesion ; cilium ; microtubule cytoskeleton ;
Biological process	tubulin complex assembly ; regulation of insulin secretion ; negative regulation of GTPase activity ; regulation of microtubule polymerization ; bicellular tight junction assembly ; positive regulation of microtubule polymerization ; cell cycle ; maintenance of protein location in nucleus ; positive regulation of cell-substrate adhesion ; centrosome cycle ;
	Sources:Amigo / QuickGO
Orthologs
	402
	56327
	ENSG00000213465
	ENSMUSG00000024944
	P36404
	Q9D0J4
	NM_001667 ; NM_001199745
	NM_019722
	NP_001186674 ; NP_001658
	NP_062696
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated May 13, 2024

ADP-ribosylation factor-like protein 2 is a protein that in humans is encoded by the ARL2 gene.^[5]^[6]^[7]

Function

The ADP-ribosylation factor (ARF) genes are small GTP-binding proteins of the RAS superfamily. ARL2 is a member of a functionally distinct group of ARF-like genes.^[7]
In photoreceptors, ARL2 participates in the trafficking of lipidated membrane-associated proteins.^[8]
There is an evidence that increased activity of ARL2 protein is strongly correlated with increased mitochondria fusion, while loss of ARL2 activity results in a decreased rate of fusion.^[9]

Interactions

ARL2 has been shown to interact with Protein unc-119 homolog,^[10] TBCD ^[11]^[12] and PDE6D.^[13]^[14]

Related Research Articles

COPI is a coatomer, a protein complex that coats vesicles transporting proteins from the cis end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally synthesized, and between Golgi compartments. This type of transport is retrograde transport, in contrast to the anterograde transport associated with the COPII protein. The name "COPI" refers to the specific coat protein complex that initiates the budding process on the cis-Golgi membrane. The coat consists of large protein subcomplexes that are made of seven different protein subunits, namely α, β, β', γ, δ, ε and ζ.

ADP-ribosylation factor 6 (ARF6) is a member of the ADP ribosylation factor family of GTP-binding proteins. ARF6 has a variety of cellular functions that are frequently involved in trafficking of biological membranes and transmembrane protein cargo. ARF6 has specifically been implicated in endocytosis of plasma membrane proteins and also, to a lesser extent, plasma membrane protein recycling.

ADP ribosylation factors (ARFs) are members of the ARF family of GTP-binding proteins of the Ras superfamily. ARF family proteins are ubiquitous in eukaryotic cells, and six highly conserved members of the family have been identified in mammalian cells. Although ARFs are soluble, they generally associate with membranes because of N-terminus myristoylation. They function as regulators of vesicular traffic and actin remodelling.

ADP-ribosylation factor 1 is a protein that in humans is encoded by the ARF1 gene.

ADP-ribosylation factor-binding protein GGA1 is a protein that in humans is encoded by the GGA1 gene.

ADP-ribosylation factor-binding protein GGA3 is a protein that in humans is encoded by the GGA3 gene.

Cytohesin-2 is a protein that in humans is encoded by the CYTH2 gene.

Cytohesin-1 formerly known as Pleckstrin homology, Sec7 and coiled/coil domains 1 (PSCD1) is a protein that in humans is encoded by the CYTH1 gene.

ADP-ribosylation factor 3 is a protein that in humans is encoded by the ARF3 gene.

Golgin subfamily A member 4 is a protein that in humans is encoded by the GOLGA4 gene.

ADP-ribosylation factor 5 is a protein that in humans is encoded by the ARF5 gene.

Uncoordinated-119 (Unc-119) is a protein that has been identified in C. elegans, humans, mice, zebrafish, rabbits, pig, calf, monkey, and protozoa. They have been classified in the GMP phosphodiesterase, delta superfamily. Unc-119 proteins are categorized into their own family but are shown to be ancestrally related to PrBP and rhoGDI. It has been given many different names: Retinal Protein 4, HRG4, POC7 Centriolar Protein Homolog A, IMD13, POC7A, and RG4.

ADP-ribosylation factor 4 is a protein that in humans is encoded by the ARF4 gene.

ADP-ribosylation factor-like protein 3 is a protein that in humans is encoded by the ARL3 gene.

ADP-ribosylation factor-like protein 1 is a protein that in humans is encoded by the ARL1 gene.

Tubulin-specific chaperone D is a protein that in humans is encoded by the TBCD gene.

Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 is a protein that in humans is encoded by the ASAP2 gene.

ADP-ribosylation factor-related protein 1 is a protein that in humans is encoded by the ARFRP1 gene.

IQ motif and SEC7 domain-containing protein 1 also known as ARF-GEP₁₀₀ (ADP-Ribosylation Factor - Guanine nucleotide-Exchange Protein - 100-kDa) is a protein that in humans is encoded by the IQSEC1 gene.

ADP-ribosylation factor-like protein 8B is a protein that in humans is encoded by the ARL8B gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000213465 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024944 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Clark J, Moore L, Krasinskas A, Way J, Battey J, Tamkun J, Kahn RA (November 1993). "Selective amplification of additional members of the ADP-ribosylation factor (ARF) family: cloning of additional human and Drosophila ARF-like genes". Proc. Natl. Acad. Sci. U.S.A. 90 (19): 8952–6. Bibcode:1993PNAS...90.8952C. doi: 10.1073/pnas.90.19.8952 . PMC 47479 . PMID 8415637.
↑ Guru SC, Agarwal SK, Manickam P, Olufemi SE, Crabtree JS, Weisemann JM, Kester MB, Kim YS, Wang Y, Emmert-Buck MR, Liotta LA, Spiegel AM, Boguski MS, Roe BA, Collins FS, Marx SJ, Burns L, Chandrasekharappa SC (September 1997). "A transcript map for the 2.8-Mb region containing the multiple endocrine neoplasia type 1 locus". Genome Res. 7 (7): 725–35. doi:10.1101/gr.7.7.725. PMC 310681 . PMID 9253601.
1 2 "Entrez Gene: ARL2 ADP-ribosylation factor-like 2".
↑ Hanke-Gogokhia, C.; Zhang, H.; Frederick, J. M.; Baehr, W. (2016). "The Function of Arf-like Proteins ARL2 and ARL3 in Photoreceptors". Retinal Degenerative Diseases. Advances in Experimental Medicine and Biology. Vol. 854. pp. 655–661. doi:10.1007/978-3-319-17121-0_87. ISBN 978-3-319-17120-3. PMID 26427472.
↑ Newman, L. E.; Schiavon, C. R.; Turn, R. E.; Kahn, R. A. (2017). "The ARL2 GTPase regulates mitochondrial fusion from the intermembrane space". Cellular Logistics. 7 (3): e1340104. doi:10.1080/21592799.2017.1340104. PMC 5602422 . PMID 28944094.
↑ Kobayashi A, Kubota S, Mori N, McLaren MJ, Inana G (January 2003). "Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a putative conserved domain". FEBS Lett. 534 (1–3): 26–32. Bibcode:2003FEBSL.534...26K. doi: 10.1016/S0014-5793(02)03766-3 . PMID 12527357. S2CID 22603052.
↑ Shern JF, Sharer JD, Pallas DC, Bartolini F, Cowan NJ, Reed MS, Pohl J, Kahn RA (October 2003). "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A". J. Biol. Chem. 278 (42): 40829–36. doi: 10.1074/jbc.M308678200 . PMID 12912990.
↑ Bhamidipati A, Lewis SA, Cowan NJ (May 2000). "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin". J. Cell Biol. 149 (5): 1087–96. doi:10.1083/jcb.149.5.1087. PMC 2174823 . PMID 10831612.
↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
↑ Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (May 2002). "The complex of Arl2-GTP and PDE delta: from structure to function". EMBO J. 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981 . PMID 11980706.

External links

Human ARL2 genome location and ARL2 gene details page in the UCSC Genome Browser .

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Bhamidipati A, Lewis SA, Cowan NJ (2000). "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin". J. Cell Biol. 149 (5): 1087–96. doi:10.1083/jcb.149.5.1087. PMC 2174823 . PMID 10831612.
Sharer JD, Shern JF, Van Valkenburgh H, Wallace DC, Kahn RA (2002). "ARL2 and BART enter mitochondria and bind the adenine nucleotide transporter". Mol. Biol. Cell. 13 (1): 71–83. doi:10.1091/mbc.01-05-0245. PMC 65073 . PMID 11809823.
Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (2002). "The complex of Arl2-GTP and PDE delta: from structure to function". EMBO J. 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981 . PMID 11980706.
Antoshechkin I, Han M (2002). "The C. elegans evl-20 gene is a homolog of the small GTPase ARL2 and regulates cytoskeleton dynamics during cytokinesis and morphogenesis". Dev. Cell. 2 (5): 579–91. doi: 10.1016/S1534-5807(02)00146-6 . PMID 12015966.
Kobayashi A, Kubota S, Mori N, McLaren MJ, Inana G (2003). "Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a putative conserved domain". FEBS Lett. 534 (1–3): 26–32. Bibcode:2003FEBSL.534...26K. doi: 10.1016/S0014-5793(02)03766-3 . PMID 12527357. S2CID 22603052.
Shern JF, Sharer JD, Pallas DC, Bartolini F, Cowan NJ, Reed MS, Pohl J, Kahn RA (2003). "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A". J. Biol. Chem. 278 (42): 40829–36. doi: 10.1074/jbc.M308678200 . PMID 12912990.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Zhou C, Cunningham L, Marcus AI, Li Y, Kahn RA (2006). "Arl2 and Arl3 regulate different microtubule-dependent processes". Mol. Biol. Cell. 17 (5): 2476–87. doi:10.1091/mbc.E05-10-0929. PMC 1446103 . PMID 16525022.
Beghin A, Honore S, Messana C, Matera EL, Aim J, Burlinchon S, Braguer D, Dumontet C (2007). "ADP ribosylation factor like 2 (Arl2) protein influences microtubule dynamics in breast cancer cells". Exp. Cell Res. 313 (3): 473–85. doi:10.1016/j.yexcr.2006.10.024. PMID 17188265.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000213465 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024944 – 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.

[pmid8415637-5] Clark J, Moore L, Krasinskas A, Way J, Battey J, Tamkun J, Kahn RA (November 1993). "Selective amplification of additional members of the ADP-ribosylation factor (ARF) family: cloning of additional human and Drosophila ARF-like genes". Proc. Natl. Acad. Sci. U.S.A. 90 (19): 8952–6. Bibcode:1993PNAS...90.8952C. doi: 10.1073/pnas.90.19.8952 . PMC 47479 . PMID 8415637.

[pmid9253601-6] Guru SC, Agarwal SK, Manickam P, Olufemi SE, Crabtree JS, Weisemann JM, Kester MB, Kim YS, Wang Y, Emmert-Buck MR, Liotta LA, Spiegel AM, Boguski MS, Roe BA, Collins FS, Marx SJ, Burns L, Chandrasekharappa SC (September 1997). "A transcript map for the 2.8-Mb region containing the multiple endocrine neoplasia type 1 locus". Genome Res. 7 (7): 725–35. doi:10.1101/gr.7.7.725. PMC 310681 . PMID 9253601.

[entrez-7] 1 2 "Entrez Gene: ARL2 ADP-ribosylation factor-like 2".

[8] Hanke-Gogokhia, C.; Zhang, H.; Frederick, J. M.; Baehr, W. (2016). "The Function of Arf-like Proteins ARL2 and ARL3 in Photoreceptors". Retinal Degenerative Diseases. Advances in Experimental Medicine and Biology. Vol. 854. pp. 655–661. doi:10.1007/978-3-319-17121-0_87. ISBN 978-3-319-17120-3. PMID 26427472.

[9] Newman, L. E.; Schiavon, C. R.; Turn, R. E.; Kahn, R. A. (2017). "The ARL2 GTPase regulates mitochondrial fusion from the intermembrane space". Cellular Logistics. 7 (3): e1340104. doi:10.1080/21592799.2017.1340104. PMC 5602422 . PMID 28944094.

[pmid12527357-10] Kobayashi A, Kubota S, Mori N, McLaren MJ, Inana G (January 2003). "Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a putative conserved domain". FEBS Lett. 534 (1–3): 26–32. Bibcode:2003FEBSL.534...26K. doi: 10.1016/S0014-5793(02)03766-3 . PMID 12527357. S2CID 22603052.

[pmid12912990-11] Shern JF, Sharer JD, Pallas DC, Bartolini F, Cowan NJ, Reed MS, Pohl J, Kahn RA (October 2003). "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A". J. Biol. Chem. 278 (42): 40829–36. doi: 10.1074/jbc.M308678200 . PMID 12912990.

[pmid10831612-12] Bhamidipati A, Lewis SA, Cowan NJ (May 2000). "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin". J. Cell Biol. 149 (5): 1087–96. doi:10.1083/jcb.149.5.1087. PMC 2174823 . PMID 10831612.

[pmid16189514-13] Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

[pmid11980706-14] Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (May 2002). "The complex of Arl2-GTP and PDE delta: from structure to function". EMBO J. 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981 . PMID 11980706.

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