Alpha catenin

catenin (cadherin-associated protein), alpha 3
Identifiers
Symbol	CTNNA3
Entrez	29119
HUGO	2511
OMIM	607667
RefSeq	NM_013266
UniProt	Q9UI47
Other data
Locus	Chr. 10 q21

catenin (cadherin-associated protein), alpha 2
Identifiers
Symbol	CTNNA2
Entrez	1496
HUGO	2510
OMIM	114025
RefSeq	NM_004389
UniProt	P26232
Other data
Locus	Chr. 2 p12-p11.1

catenin (cadherin-associated protein), alpha 1, 102kDa
	File:Catenin Alpha-1.png Model of human aldehyde oxidase after PDB: 1H6G
Identifiers
Symbol	CTNNA1
Entrez	1495
HUGO	2509
OMIM	116805
RefSeq	NM_001903
UniProt	P35221
Other data
Locus	Chr. 5 q31.2

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

There are three human alpha-catenin genes:

alpha-1-catenin (also called alpha-E-catenin)
alpha-2-catenin (also called alpha-N-catenin)
alpha-3-catenin (also called alpha-T-catenin)

External links

alpha+Catenin at the US National Library of Medicine Medical Subject Headings (MeSH)

References

↑ 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 0-87893-219-4.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.

This article on a gene on human chromosome 10 is a stub. You can help Wikipedia by expanding it.

[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 0-87893-219-4.

[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.

[pmid30037495-6] 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.

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Alpha catenin

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Types

See also

External links

References

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catenin (cadherin-associated protein), alpha 1, 102kDa
File:Catenin Alpha-1.png Model of human aldehyde oxidase after PDB: 1H6G
Identifiers
Symbol	CTNNA1
Entrez	1495
HUGO	2509
OMIM	116805
RefSeq	NM_001903
UniProt	P35221
Other data
Locus	Chr. 5 q31.2