Alpha catenin

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catenin (cadherin-associated protein), alpha 1, 102kDa
Catenin Alpha-1.png
Model of human aldehyde oxidase after PDB: 1H6G
Identifiers
SymbolCTNNA1
Entrez1495
HUGO2509
OMIM116805
RefSeqNM_001903
UniProtP35221
Other data
LocusChr. 5 q31.2
catenin (cadherin-associated protein), alpha 2
Identifiers
SymbolCTNNA2
Entrez1496
HUGO2510
OMIM114025
RefSeqNM_004389
UniProtP26232
Other data
LocusChr. 2 p12-p11.1
catenin (cadherin-associated protein), alpha 3
Identifiers
SymbolCTNNA3
Entrez29119
HUGO2511
OMIM607667
RefSeqNM_013266
UniProtQ9UI47
Other data
LocusChr. 10 q21

Alpha-catenin was proposed to function as a linking protein between cadherins and actin-containing filaments of the cytoskeleton.[1] It has been reported that the actin binding proteins vinculin[2] and alpha-actinin[3] can bind to alpha-catenin. However, a protein complex including a cadherin, actin, beta-catenin and alpha-catenin has not been isolated.[citation needed] It has been suggested that alpha-catenin does not bind with high affinity to both actin filaments and the E-cadherin-beta-catenin complex at the same time.[4] It has been observed that when alpha-catenin is not in a molecular complex with beta-catenin, it dimerizes and functions to regulate actin filament assembly, possibly by competing with Arp2/3 protein.[5] Alpha catenin exhibits significant protein dynamics.[6]

The amino acid sequence of alpha-catenin has sequence similarity to that of vinculin.[7]

Types[edit]

There are three human alpha-catenin genes:

  • CTNNA1, alpha-1-catenin (also called alpha-E-catenin)
  • CTNNA2, alpha-2-catenin (also called alpha-N-catenin)
  • CTNNA3, alpha-3-catenin (also called alpha-T-catenin)

See also[edit]

External links[edit]

References[edit]

  1. ^ Cooper, Geoffrey M. (2000). "Figure 11.14: Model of attachment of actin filaments to catenin-cadherin complexes". The Cell: A Molecular Approach (2nd ed.). Sinauer Associates. ISBN 978-0-87893-219-1.
  2. ^ Watabe-Uchida M, Uchida N, Imamura Y, et al. (August 1998). "alpha-Catenin-vinculin interaction functions to organize the apical junctional complex in epithelial cells". J. Cell Biol. 142 (3): 847–57. doi:10.1083/jcb.142.3.847. hdl:1854/LU-151543. PMC 2148175. PMID 9700171.
  3. ^ Knudsen KA, Soler AP, Johnson KR, Wheelock MJ (July 1995). "Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin". J. Cell Biol. 130 (1): 67–77. doi:10.1083/jcb.130.1.67. PMC 2120515. PMID 7790378.
  4. ^ Yamada S, Pokutta S, Drees F, Weis WI, Nelson WJ (December 2005). "Deconstructing the cadherin-catenin-actin complex". Cell. 123 (5): 889–901. doi:10.1016/j.cell.2005.09.020. PMC 3368712. PMID 16325582.
  5. ^ Drees F, Pokutta S, Yamada S, Nelson WJ, Weis WI (December 2005). "Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly". Cell. 123 (5): 903–15. doi:10.1016/j.cell.2005.09.021. PMC 3369825. PMID 16325583.
  6. ^ Nicholl ID, Matsui T, Weiss TM, Stanley CB, Heller WT, Martel A, Farago B, Callaway DJ, Bu Z (Aug 21, 2018). "Alpha-catenin structure and nanoscale dynamics in solution and in complex with F-actin". Biophysical Journal. 115 (4): 642–654. doi:10.1016/j.bpj.2018.07.005. PMC 6104293. PMID 30037495.
  7. ^ Nagafuchi A, Takeichi M, Tsukita S (May 1991). "The 102 kd cadherin-associated protein: similarity to vinculin and posttranscriptional regulation of expression". Cell. 65 (5): 849–57. doi:10.1016/0092-8674(91)90392-C. PMID 1904011.