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Alpha-actinin-4

From Wikipedia, the free encyclopedia

ACTN4
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesACTN4, ACTININ-4, FSGS, FSGS1, Actinin alpha 4
External IDsOMIM: 604638; MGI: 1890773; HomoloGene: 55857; GeneCards: ACTN4; OMA:ACTN4 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004924
NM_001322033

NM_021895
NM_001360548
NM_001360549
NM_001360550

RefSeq (protein)

NP_001308962
NP_004915

NP_068695
NP_001347477
NP_001347478
NP_001347479

Location (UCSC)Chr 19: 38.65 – 38.73 MbChr 7: 28.59 – 28.66 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Alpha-actinin-4 is a protein that in humans is encoded by the ACTN4 gene.[5]

Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments. This gene encodes a nonmuscle, alpha actinin isoform which is concentrated in the cytoplasm, and thought to be involved in metastatic processes. Mutations in this gene have been associated with focal and segmental glomerulosclerosis.[5]

Interactions

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Alpha-actinin-4 has been shown to interact with PDLIM1,[6][7] Sodium-hydrogen exchange regulatory cofactor 2,[8] Collagen, type XVII, alpha 1,[9] CAMK2A,[10] CAMK2B,[10] MAGI1[11] and TRIM3.[12]

See also

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References

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  1. ^ a b c ENSG00000282844 GRCh38: Ensembl release 89: ENSG00000130402, ENSG00000282844Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000054808Ensembl, 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. ^ a b "Entrez Gene: ACTN4 actinin, alpha 4".
  6. ^ Rual JF, Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062). England: 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  7. ^ Vallenius T, Luukko K, Mäkelä T P (Apr 2000). "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4". J. Biol. Chem. 275 (15). UNITED STATES: 11100–5. doi:10.1074/jbc.275.15.11100. ISSN 0021-9258. PMID 10753915.
  8. ^ Kim JH, Lee-Kwon Whaseon, Park Jong Bae, Ryu Sung Ho, Yun C H Chris, Donowitz Mark (Jun 2002). "Ca(2+)-dependent inhibition of Na+/H+ exchanger 3 (NHE3) requires an NHE3-E3KARP-alpha-actinin-4 complex for oligomerization and endocytosis". J. Biol. Chem. 277 (26). United States: 23714–24. doi:10.1074/jbc.M200835200. ISSN 0021-9258. PMID 11948184.
  9. ^ Gonzalez AM, Otey C, Edlund M, Jones J C (Dec 2001). "Interactions of a hemidesmosome component and actinin family members". J. Cell Sci. 114 (Pt 23). England: 4197–206. doi:10.1242/jcs.114.23.4197. ISSN 0021-9533. PMID 11739652.
  10. ^ a b Walikonis RS, Oguni A, Khorosheva E M, Jeng C J, Asuncion F J, Kennedy M B (Jan 2001). "Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin". J. Neurosci. 21 (2). United States: 423–33. doi:10.1523/JNEUROSCI.21-02-00423.2001. PMC 6763799. PMID 11160423.
  11. ^ Patrie KM, Drescher Andrew J, Welihinda Ajith, Mundel Peter, Margolis Ben (Aug 2002). "Interaction of two actin-binding proteins, synaptopodin and alpha-actinin-4, with the tight junction protein MAGI-1". J. Biol. Chem. 277 (33). United States: 30183–90. doi:10.1074/jbc.M203072200. ISSN 0021-9258. PMID 12042308.
  12. ^ El-Husseini AE, Kwasnicka D, Yamada T, Hirohashi S, Vincent S R (Jan 2000). "BERP, a novel ring finger protein, binds to alpha-actinin-4". Biochem. Biophys. Res. Commun. 267 (3). UNITED STATES: 906–11. doi:10.1006/bbrc.1999.2045. ISSN 0006-291X. PMID 10673389.

Further reading

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