Actin-binding domain of mouse plectin. Crystal structure and
binding to vimentin

J 2005

Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin

ŠEVČÍK, Jozef, Lubica URBÁNIKOVÁ, Július KOŠŤAN, Lubomír JANDA, Gerhard WICHE et. al.

Basic information

Original name

Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin

Name in Czech

Aktin vazebná doména myšího plektinu. Krystalová struktura a vazba k vimentinu

Authors

ŠEVČÍK, Jozef (703 Slovakia), Lubica URBÁNIKOVÁ (703 Slovakia), Július KOŠŤAN (703 Slovakia), Lubomír JANDA (203 Czech Republic, guarantor) and Gerhard WICHE (40 Austria)

Edition

1873-84, Oxford, Blackwell Science, 2005, 0014-2956

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

Austria

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 3.164

RIV identification code

RIV/00216224:14310/05:00039944

Organization unit

Faculty of Science

UT WoS

000221135700008

Keywords (in Czech)

Aktin vazebná doména; vimentin; plektin

Keywords in English

Actin binding domain; vimentin; plectin

Změněno: 9/4/2010 15:49, RNDr. Lubomír Janda, Ph.D.

Abstract

V originále

Plectin, a large and widely expressed cytolinker protein, is composed of several subdomains that harbor binding sites for a variety of different interaction partners. A canonical actin-binding domain (ABD) comprising two calponin homology domains (CH1 and CH2) is located in proximity to its amino terminus. However, the ABD of plectin is unique among actin-binding proteins as it is expressed in the form of distinct, plectin isoform-specific versions. We have determined the three-dimensional structure of two distinct crystalline forms of one of its ABD versions (pleABD/2alpha) from mouse, to a resolution of 1.95 and 2.0 A. Comparison of pleABD/2alpha with the ABDs of fimbrin and utrophin revealed structural similarity between plectin and fimbrin, although the proteins share only low sequence identity. In fact, pleABD/2alpha has been found to have the same compact fold as the human plectin ABD and the fimbrin ABD, differing from the open conformation described for the ABDs of utrophin and dystrophin. Plectin harbors a specific binding site for intermediate filaments of various types within its carboxy-terminal R5 repeat domain. Our experiments revealed an additional vimentin-binding site of plectin, residing within the CH1 subdomain of its ABD. We show that vimentin binds to this site via the amino-terminal part of its rod domain. This additional amino-terminal intermediate filament protein binding site of plectin may have a function in intermediate filament dynamics and assembly, rather than in linking and stabilizing intermediate filament networks.

Links

MSM0021622415, plan (intention)

Name: Molekulární podstata buněčných a tkáňových regulací

Investor: Ministry of Education, Youth and Sports of the CR, Molecular basis of cell and tissue regulations

Citovat

ŠEVČÍK, Jozef, Lubica URBÁNIKOVÁ, Július KOŠŤAN, Lubomír JANDA and Gerhard WICHE. Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin. 1873-84. Oxford: Blackwell Science, 2005, vol. 271, No 10, p. 1873-1884, 2004 pp. ISSN 0014-2956.

@article{879440,
   author = {Ševčík, Jozef and Urbániková, Lubica and Košťan, Július and Janda, Lubomír and Wiche, Gerhard},
   article_location = {Oxford},
   article_number = {10},
   keywords = {Actin binding domain; vimentin; plectin},
   language = {eng},
   issn = {0014-2956},
   journal = {1873-84},
   title = {Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin},
   volume = {271},
   year = {2005}
}

TY  - JOUR
ID  - 879440
AU  - Ševčík, Jozef - Urbániková, Lubica - Košťan, Július - Janda, Lubomír - Wiche, Gerhard
PY  - 2005
TI  - Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin
JF  - 1873-84
VL  - 271
IS  - 10
SP  - 1873-1884
EP  - 1873-1884
PB  - Blackwell Science
SN  - 00142956
KW  - Actin binding domain
KW  - vimentin
KW  - plectin
N2  - Plectin, a large and widely expressed cytolinker protein, is composed of several subdomains that harbor binding sites for a variety of different interaction partners. A canonical actin-binding domain (ABD) comprising two calponin homology domains (CH1 and CH2) is located in proximity to its amino terminus. However, the ABD of plectin is unique among actin-binding proteins as it is expressed in the form of distinct, plectin isoform-specific versions. We have determined the three-dimensional structure of two distinct crystalline forms of one of its ABD versions (pleABD/2alpha) from mouse, to a resolution of 1.95 and 2.0 A. Comparison of pleABD/2alpha with the ABDs of fimbrin and utrophin revealed structural similarity between plectin and fimbrin, although the proteins share only low sequence identity. In fact, pleABD/2alpha has been found to have the same compact fold as the human plectin ABD and the fimbrin ABD, differing from the open conformation described for the ABDs of utrophin and dystrophin. Plectin harbors a specific binding site for intermediate filaments of various types within its carboxy-terminal R5 repeat domain. Our experiments revealed an additional vimentin-binding site of plectin, residing within the CH1 subdomain of its ABD. We show that vimentin binds to this site via the amino-terminal part of its rod domain. This additional amino-terminal intermediate filament protein binding site of plectin may have a function in intermediate filament dynamics and assembly, rather than in linking and stabilizing intermediate filament networks.
ER  -

ŠEVČÍK, Jozef, Lubica URBÁNIKOVÁ, Július KOŠŤAN, Lubomír JANDA and Gerhard WICHE. Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin. \textit{1873-84}. Oxford: Blackwell Science, 2005, vol.~271, No~10, p.~1873-1884, 2004 pp. ISSN~0014-2956.

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