Actinin alpha 4

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

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RefSeq (protein)

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Alpha-actinin-4 is a protein that in humans is encoded by the ACTN4 gene.[1]

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.[1]

Interactions

Actinin alpha 4 has been shown to interact with PDLIM1,[2][3] Sodium-hydrogen exchange regulatory cofactor 2,[4] Collagen, type XVII, alpha 1,[5] CAMK2A,[6] CAMK2B,[6] MAGI1[7] and TRIM3.[8]

See also

References

  1. 1.0 1.1 "Entrez Gene: ACTN4 actinin, alpha 4".
  2. Rual, Jean-François; 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. England. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.
  3. 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. UNITED STATES. 275 (15): 11100–5. doi:10.1074/jbc.275.15.11100. ISSN 0021-9258. PMID 10753915.
  4. Kim, Jae Ho; 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. United States. 277 (26): 23714–24. doi:10.1074/jbc.M200835200. ISSN 0021-9258. PMID 11948184.
  5. Gonzalez, A M; Otey C; Edlund M; Jones J C (Dec 2001). "Interactions of a hemidesmosome component and actinin family members". J. Cell Sci. England. 114 (Pt 23): 4197–206. ISSN 0021-9533. PMID 11739652.
  6. 6.0 6.1 Walikonis, R S; 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. United States. 21 (2): 423–33. PMID 11160423.
  7. Patrie, Kevin M; 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. United States. 277 (33): 30183–90. doi:10.1074/jbc.M203072200. ISSN 0021-9258. PMID 12042308.
  8. El-Husseini, A E; 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. UNITED STATES. 267 (3): 906–11. doi:10.1006/bbrc.1999.2045. ISSN 0006-291X. PMID 10673389.

Further reading

External links