Actinin alpha 4

From Wikipedia, the free encyclopedia

Actinin, alpha 4

PDB rendering based on 1wlx.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1WLX, 2R0O

Identifiers

Symbols

ACTN4; ACTININ-4; FSGS; FSGS1

External IDs

OMIM: 604638 MGI: 1890773 HomoloGene: 55857 GeneCards: ACTN4 Gene

Gene Ontology
Molecular function	• nucleoside binding • actin binding • integrin binding • calcium ion binding • protein binding • protein homodimerization activity • protein N-terminus binding • actin filament binding
Cellular component	• extracellular region • nucleus • cytoplasm • Z disc • ribonucleoprotein complex • cortical cytoskeleton • platelet alpha granule lumen • pseudopodium • protein complex • perinuclear region of cytoplasm • extracellular vesicular exosome
Biological process	• response to hypoxia • platelet degranulation • blood coagulation • protein transport • platelet activation • positive regulation of sodium:hydrogen antiporter activity • regulation of apoptotic process • positive regulation of pinocytosis • actin filament bundle assembly • negative regulation of cellular component movement • positive regulation of cellular component movement • actin crosslink formation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
39.14 – 39.22 Mb

Chr 7:
28.89 – 28.96 Mb

PubMed search

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]

References

↑ 1.0 1.1 "Entrez Gene: ACTN4 actinin, alpha 4".
↑ 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. doi:10.1038/nature04209. PMID 16189514. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)
↑ 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. Cite uses deprecated parameters (help)

Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
Yürüker B, Niggli V (1992). "Alpha-actinin and vinculin in human neutrophils: reorganization during adhesion and relation to the actin network.". J. Cell. Sci. 101. ( Pt 2): 403–14. PMID 1629252.
Otey CA, Pavalko FM, Burridge K (1990). "An interaction between alpha-actinin and the beta 1 integrin subunit in vitro.". J. Cell Biol. 111 (2): 721–9. doi:10.1083/jcb.111.2.721. PMC 2116186. PMID 2116421.
Pavalko FM, LaRoche SM (1993). "Activation of human neutrophils induces an interaction between the integrin beta 2-subunit (CD18) and the actin binding protein alpha-actinin.". J. Immunol. 151 (7): 3795–807. PMID 8104223.
Mathis BJ, Kim SH, Calabrese K, et al. (1998). "A locus for inherited focal segmental glomerulosclerosis maps to chromosome 19q13.". Kidney Int. 53 (2): 282–6. doi:10.1046/j.1523-1755.1998.00828.x. PMID 9461087.
Honda K, Yamada T, Endo R, et al. (1998). "Actinin-4, a novel actin-bundling protein associated with cell motility and cancer invasion.". J. Cell Biol. 140 (6): 1383–93. doi:10.1083/jcb.140.6.1383. PMC 2132673. PMID 9508771.
Zhang H, Wang L, Kao S, et al. (1999). "Functional interaction between the cytoplasmic leucine-zipper domain of HIV-1 gp41 and p115-RhoGEF.". Curr. Biol. 9 (21): 1271–4. doi:10.1016/S0960-9822(99)80511-9. PMID 10556093.
Nikolopoulos SN, Spengler BA, Kisselbach K, et al. (2000). "The human non-muscle alpha-actinin protein encoded by the ACTN4 gene suppresses tumorigenicity of human neuroblastoma cells.". Oncogene 19 (3): 380–6. doi:10.1038/sj.onc.1203310. PMID 10656685.
El-Husseini AE, Kwasnicka D, Yamada T, et al. (2000). "BERP, a novel ring finger protein, binds to alpha-actinin-4.". Biochem. Biophys. Res. Commun. 267 (3): 906–11. doi:10.1006/bbrc.1999.2045. PMID 10673389.
Kaplan JM, Kim SH, North KN, et al. (2000). "Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal segmental glomerulosclerosis.". Nat. Genet. 24 (3): 251–6. doi:10.1038/73456. PMID 10700177.
Vallenius T, Luukko K, Mäkelä TP (2000). "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4.". J. Biol. Chem. 275 (15): 11100–5. doi:10.1074/jbc.275.15.11100. PMID 10753915.
Holliday LS, Lu M, Lee BS, et al. (2000). "The amino-terminal domain of the B subunit of vacuolar H+-ATPase contains a filamentous actin binding site.". J. Biol. Chem. 275 (41): 32331–7. doi:10.1074/jbc.M004795200. PMID 10915794.
Walikonis RS, Oguni A, Khorosheva EM, et al. (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): 423–33. PMID 11160423.
Echchakir H, Mami-Chouaib F, Vergnon I, et al. (2001). "A point mutation in the alpha-actinin-4 gene generates an antigenic peptide recognized by autologous cytolytic T lymphocytes on a human lung carcinoma.". Cancer Res. 61 (10): 4078–83. PMID 11358829.
Xu F, Zhao R, Peng Y, et al. (2001). "Association of tyrosine phosphatase SHP-2 with F-actin at low cell densities.". J. Biol. Chem. 276 (31): 29479–84. doi:10.1074/jbc.M104428200. PMID 11382784.
Hüttelmaier S, Illenberger S, Grosheva I, et al. (2002). "Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and microfilament attachment proteins.". J. Cell Biol. 155 (5): 775–86. doi:10.1083/jcb.200105044. PMC 2150882. PMID 11724819.
Renoult C, Blondin L, Fattoum A, et al. (2002). "Binding of gelsolin domain 2 to actin. An actin interface distinct from that of gelsolin domain 1 and from ADF/cofilin.". Eur. J. Biochem. 268 (23): 6165–75. doi:10.1046/j.0014-2956.2001.02574.x. PMID 11733011.
Gonzalez AM, Otey C, Edlund M, Jones JC (2002). "Interactions of a hemidesmosome component and actinin family members.". J. Cell. Sci. 114 (Pt 23): 4197–206. PMID 11739652.
Lukoyanova N, VanLoock MS, Orlova A, et al. (2002). "Each actin subunit has three nebulin binding sites: implications for steric blocking.". Curr. Biol. 12 (5): 383–8. doi:10.1016/S0960-9822(02)00678-4. PMID 11882289.
Kim JH, Lee-Kwon W, Park JB, et al. (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): 23714–24. doi:10.1074/jbc.M200835200. PMID 11948184.

PDB gallery

1wlx: Solution structure of the third spectrin repeat of alpha-actinin-4

2eyi: Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.7 Angstrom resolution

2eyn: Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom resolution

Proteins of the cytoskeleton

Human

Microfilaments
(ABPs)

Myofilament

Actins	A1 A2 B C1 G1 G2

Myosins	I MYO1A MYO1B MYO1C MYO1D MYO1E MYO1F MYO1G MYO1H) II MYH1 MYH2 MYH3 MYH4 MYH6 MYH7 MYH7B MYH8 MYH9 MYH10 MYH11 MYH13 MYH14 MYH15 MYH16 III MYO3A MYO3B V MYO5A MYO5B MYO5C VI MYO6 VII MYO7A MYO7B IX MYO9A MYO9B X MYO10 XV MYO15A XVIII MYO18A MYO18B LC MYL1 MYL2 MYL3 MYL4 MYL5 MYL6 MYL6B MYL7 MYL9 MYLIP MYLK MYLK2 MYLL1

Other	Tropomodulin 1 2 3 4 Troponin T 1 2 3 C 1 2 I 1 2 3 Tropomyosin 1 2 3 4 Actinin 1 2 3 4 Arp2/3 complex actin depolymerizing factors Cofilin 1 2 Destrin Gelsolin Profilin 1 2 Titin

Other

IFs

Type 1/2
(Keratin,
Cytokeratin)

Epithelial keratins (soft alpha-keratins)	type I/chromosome 17 10 12 13 14 15 16 17 19 20 chromosome 12 18 none 21 type II/chromosome 12 1 2A 3 4 5 6A 6B 7 8 9

Hair keratins (hard alpha-keratins)	type I/chromosome 17 31 32 33A 33B 34 35 36 37 38 type II/chromosome 12 81 82 83 84 85 86

Ungrouped alpha	chromosome 17 23 24 25 26 27 28 39 40 chromosome 12 71 72 73 74 75 76 77 78 79 80

Not alpha	Beta-keratin

Type 3

Type 4

Type 5

Lamin A
B

Microtubules/
MAPs

Kinesins	KIF1A KIF1B KIF2A KIF2C KIF3B KIF3C KIF4A KIF4B KIF5A KIF5B KIF5C KIF6 KIF7 KIF9 KIF11 KIF12 KIF13A KIF13B KIF14 KIF15 KIF16B KIF17 KIF18A KIF18B KIF19 KIF20A KIF20B KIF21A KIF21B KIF22 KIF23 KIF24 KIF25 KIF26A KIF26B KIF27 KIFC1 KIFC2 KIFC3

Dyneins	axonemal: DNAH1 DNAH2 DNAH3 DNAH5 DNAH6 DNAH7 DNAH8 DNAH9 DNAH10 DNAH11 DNAH12 DNAH13 DNAH14 DNAH17 DNAI1 DNAI2 DNALI1 DNAL1 DNAL4 cytoplasmic: DYNC1H1 DYNC2H1 DYNC1I1 DYNC1I2 DYNC1LI1 DYNC1LI2 DYNC2LI1 DYNLL1 DYNLL2 DYNLRB1 DYNLRB2 DYNLT1 DYNLT3

Other	Tau protein Dynactin DCTN1 Tubulins TUBA1A TUBA1B TUBA1C TUBA3C TUBA3D TUBA3E TUBA4A TUBA8 Stathmin Tektin TEKT1 TEKT2 TEKT3 TEKT4 TEKT5 Dynamin DNM1 DNM2 DNM3

Catenins

Membrane

Dystrophin
- Dystroglycan
Utrophin
Ankyrin
- ANK1
- ANK2
- ANK3
Spectrin
- SPTA1
- SPTAN1
- SPTB
- SPTBN1
- SPTBN2
- SPTBN4
- SPTBN5

Other

Nonhuman

See also: cytoskeletal defects B strc: edmb (perx), skel (ctrs), epit, cili, mito, nucl (chro)

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Actinin alpha 4

Interactions

See also

References

Further reading