Alpha catenin: Difference between revisions

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'''Alpha-catenin''' was suggested to function as a linking protein between [[cadherin]]s and [[Microfilament|actin-containing filaments]] of the [[cytoskeleton]].<ref>{{cite book |author =Cooper, Geoffrey M. |title=The Cell: A Molecular Approach |publisher=Sinauer Associates |edition=2nd |year=2000 |isbn=0-87893-219-4 |chapterurl=https://www.ncbi.nlm.nih.gov/books/NBK9908/figure/A1784/ |chapter=Figure 11.14: Model of attachment of actin filaments to catenin-cadherin complexes |url=https://www.ncbi.nlm.nih.gov/books/n/cooper/TOC/ }}</ref> It has been reported that the actin binding proteins [[vinculin]]<ref>{{cite journal |vauthors =Watabe-Uchida M, Uchida N, Imamura Y |title=alpha-Catenin-vinculin interaction functions to organize the apical junctional complex in epithelial cells |journal=J. Cell Biol. |volume=142 |issue=3 |pages=847–57 |date=August 1998 |pmid=9700171 |pmc=2148175 |url=http://www.jcb.org/cgi/pmidlookup?view=long&pmid=9700171 |doi=10.1083/jcb.142.3.847|display-authors=etal}}</ref> and alpha-actinin<ref>{{cite journal |vauthors =Knudsen KA, Soler AP, Johnson KR, Wheelock MJ |title=Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin |journal=J. Cell Biol. |volume=130 |issue=1 |pages=67–77 |date=July 1995 |pmid=7790378 |pmc=2120515 |url=http://www.jcb.org/cgi/pmidlookup?view=long&pmid=7790378 |doi=10.1083/jcb.130.1.67}}</ref> can bind to alpha-catenin. However, a protein complex including a cadherin, actin, [[beta-catenin]] and alpha-catenin has not been isolated. 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.<ref>{{cite journal |vauthors =Yamada S, Pokutta S, Drees F, Weis WI, Nelson WJ |title=Deconstructing the cadherin-catenin-actin complex |journal=Cell |volume=123 |issue=5 |pages=889–901 |date=December 2005 |pmid=16325582 |doi=10.1016/j.cell.2005.09.020 |url=http://linkinghub.elsevier.com/retrieve/pii/S0092-8674(05)00974-8 |pmc=3368712}}</ref> 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]].<ref>{{cite journal |vauthors =Drees F, Pokutta S, Yamada S, Nelson WJ, Weis WI |title=Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly |journal=Cell |volume=123 |issue=5 |pages=903–15 |date=December 2005 |pmid=16325583 |doi=10.1016/j.cell.2005.09.021 |url=http://linkinghub.elsevier.com/retrieve/pii/S0092-8674(05)00975-X |pmc=3369825}}</ref>
'''Alpha-catenin''' was proposed to function as a linking protein between [[cadherin]]s and [[Microfilament|actin-containing filaments]] of the [[cytoskeleton]].<ref>{{cite book |author =Cooper, Geoffrey M. |title=The Cell: A Molecular Approach |publisher=Sinauer Associates |edition=2nd |year=2000 |isbn=0-87893-219-4 |chapterurl=https://www.ncbi.nlm.nih.gov/books/NBK9908/figure/A1784/ |chapter=Figure 11.14: Model of attachment of actin filaments to catenin-cadherin complexes |url=https://www.ncbi.nlm.nih.gov/books/n/cooper/TOC/ }}</ref> It has been reported that the actin binding proteins [[vinculin]]<ref>{{cite journal |vauthors =Watabe-Uchida M, Uchida N, Imamura Y |title=alpha-Catenin-vinculin interaction functions to organize the apical junctional complex in epithelial cells |journal=J. Cell Biol. |volume=142 |issue=3 |pages=847–57 |date=August 1998 |pmid=9700171 |pmc=2148175 |url=http://www.jcb.org/cgi/pmidlookup?view=long&pmid=9700171 |doi=10.1083/jcb.142.3.847|display-authors=etal|hdl=1854/LU-151543 }}</ref> and alpha-actinin<ref>{{cite journal |vauthors =Knudsen KA, Soler AP, Johnson KR, Wheelock MJ |title=Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin |journal=J. Cell Biol. |volume=130 |issue=1 |pages=67–77 |date=July 1995 |pmid=7790378 |pmc=2120515 |url=http://www.jcb.org/cgi/pmidlookup?view=long&pmid=7790378 |doi=10.1083/jcb.130.1.67}}</ref> can bind to alpha-catenin. However, a protein complex including a cadherin, actin, [[beta-catenin]] and alpha-catenin has not been isolated.{{fact|date=August 2018}} 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.<ref>{{cite journal |vauthors =Yamada S, Pokutta S, Drees F, Weis WI, Nelson WJ |title=Deconstructing the cadherin-catenin-actin complex |journal=Cell |volume=123 |issue=5 |pages=889–901 |date=December 2005 |pmid=16325582 |doi=10.1016/j.cell.2005.09.020 |url=http://linkinghub.elsevier.com/retrieve/pii/S0092-8674(05)00974-8 |pmc=3368712}}</ref> 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]].<ref>{{cite journal |vauthors =Drees F, Pokutta S, Yamada S, Nelson WJ, Weis WI |title=Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly |journal=Cell |volume=123 |issue=5 |pages=903–15 |date=December 2005 |pmid=16325583 |doi=10.1016/j.cell.2005.09.021 |url=http://linkinghub.elsevier.com/retrieve/pii/S0092-8674(05)00975-X |pmc=3369825}}</ref> Alpha catenin exhibits significant [[protein dynamics]].<ref name="pmid30037495">{{cite journal | vauthors = Nicholl ID, Matsui T, Weiss TM, Stanley CB,  Heller WT, Martel A, Farago B, Callaway DJ, Bu Z | title = Alpha-catenin structure and nanoscale dynamics in solution and in complex with F-actin | journal = Biophysical Journal | volume = 115 | issue = 4  | pages = 642-654 | date =  Aug 21, 2018 | pmid = 30037495 | pmc = 6104293 | doi = 10.1016/j.bpj.2018.07.005 | url = https://www.cell.com/biophysj/fulltext/S0006-3495(18)30769-0 }}</ref>


The amino acid sequence of alpha-catenin has sequence similarity to that of [[vinculin]].<ref>{{cite journal |vauthors =Nagafuchi A, Takeichi M, Tsukita S |title=The 102 kd cadherin-associated protein: similarity to vinculin and posttranscriptional regulation of expression |journal=Cell |volume=65 |issue=5 |pages=849–57 |date=May 1991 |pmid=1904011 |url=http://linkinghub.elsevier.com/retrieve/pii/0092-8674(91)90392-C |doi=10.1016/0092-8674(91)90392-C}}</ref>
The amino acid sequence of alpha-catenin has sequence similarity to that of [[vinculin]].<ref>{{cite journal |vauthors =Nagafuchi A, Takeichi M, Tsukita S |title=The 102 kd cadherin-associated protein: similarity to vinculin and posttranscriptional regulation of expression |journal=Cell |volume=65 |issue=5 |pages=849–57 |date=May 1991 |pmid=1904011 |url=http://linkinghub.elsevier.com/retrieve/pii/0092-8674(91)90392-C |doi=10.1016/0092-8674(91)90392-C}}</ref>

Latest revision as of 13:59, 4 November 2018

catenin (cadherin-associated protein), alpha 1, 102kDa
File: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

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)

See also

External links

References

  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.
  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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