Simulation of Alpha-actinin Migration During Cell Deformation

Channel: JohnsHopkinsMedicine   |   2013/10/15
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Simulation of Alpha-actinin Migration During Cell Deformation
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RESULTS [39 .. 89]
From Wikipedia, the free encyclopedia
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Actinin, alpha 4

PDB rendering based on 1wlx.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ACTN4 ; ACTININ-4; FSGS; FSGS1
External IDs OMIM604638 MGI1890773 HomoloGene55857 GeneCards: ACTN4 Gene
RNA expression pattern
PBB GE ACTN4 200601 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 81 60595
Ensembl ENSG00000130402 ENSMUSG00000054808
UniProt O43707 P57780
RefSeq (mRNA) NM_004924 NM_021895
RefSeq (protein) NP_004915 NP_068695
Location (UCSC) Chr 19:
39.14 – 39.22 Mb
Chr 7:
28.89 – 28.96 Mb
PubMed search [1] [2]

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[edit]

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[edit]

References[edit]

  1. ^ a b "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. 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. ^ a b 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[edit]



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