Hostname: page-component-586b7cd67f-g8jcs Total loading time: 0 Render date: 2024-12-01T10:32:13.100Z Has data issue: false hasContentIssue false
  • English
  • Français

Actin Filaments Decorated with Cytoskeletal Proteins

Published online by Cambridge University Press:  02 July 2020

D. Hanein ,
S. Goldsmith ,
W. Lehman ,
R. Craig ,
I. Correia ,
P. Matsudaira ,
D.J. DeRosier  and
S.C. Almo
D. Hanein
Affiliation:
The W.M. Keck Inst, for Cellular Visualization, Brandeis Univ., Waltham, MA, 02254
S. Goldsmith
Affiliation:
Dept. Biochem., Albert Einstein Coll. Med., Bronx, NY, 10461
W. Lehman
Affiliation:
Dept. Physiol., Boston University School of Medicine, Boston, MA, 02118
R. Craig
Affiliation:
Dept. Cell Biol., Univ. Mass. Med. School, Worcester, MA, 01655
I. Correia
Affiliation:
Whitehead Institute for Biomedical Research, Cambridge, MA, 02142
P. Matsudaira
Affiliation:
Whitehead Institute for Biomedical Research, Cambridge, MA, 02142
D.J. DeRosier
Affiliation:
The W.M. Keck Inst, for Cellular Visualization, Brandeis Univ., Waltham, MA, 02254
S.C. Almo
Affiliation:
Dept. Biochem., Albert Einstein Coll. Med., Bronx, NY, 10461
Get access

Extract

A superfamily of actin crosslinking proteins, the calponin-homology domain (CH) family is implicated in directing the assembly and controlling the organization of the cytoskeleton through a highly conserved actin binding domain (ABD). This domain, composed of a tandem pair of CH motifs, is found in actin crosslinking proteins such as fimbrin, alpha-actinin, spectrin, and dystrophin. In addition to its role in crosslinking actin filaments, a putative homologous ABD in intermediate filament-binding proteins, plectin, dystonin, and BPAGlnl, suggests a possible role in crosslinks between desmosomal and vimentin intermediate filaments and actin. Thus, the CH domain could integrate the functions of the actin and IF cytoskeletons by physically linking these structural systems. We present an atomic model for the complex of the CH domain and actin.

In crosslinking proteins that organize actin into two and three dimensional networks or gels the ABDs lie at the ends of long, flexible molecules.

Type
High Resolution Protein Structures from Electron Crystallography
Information
Microscopy and Microanalysis , Volume 4 , Issue S2: Proceedings: Microscopy & Microanalysis '98, Microscopy Society of America 56th Annual Meeting, Microbeam Analysis Society 32nd Annual Meeting, Atlanta, Georgia July 12-16, 1998 , July 1998 , pp. 458 - 459
Copyright
Copyright © Microscopy Society of America

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

References:

[1]Goldsmith, S.C., Pokala, N., Shen, W., Fedorov, A.A., Matsudaira, P., Almo, S.C., Nat Struct Biol 4 (1997) 708–712 .CrossRefGoogle Scholar
[2]Hanein, D., Matsudaira, P., DeRosier, D.J., J Cell Biol 139 (1997) 387–396 .CrossRefGoogle Scholar
[3]Hanein, D., Goldsmith, S., Lehman, W., Craig, R., Matsudaira, P., DeRosier, D.J., Almo, S.C., (in prep.).Google Scholar
[4]McGough, A., Way, M., DeRosier, D., J. Cell Biol. 126 (1994) 433–443 .CrossRefGoogle Scholar
[5]Hodgkinson, J.L., el-Mezgueldi, M., Craig, R., Vibert, P., Marston, S.B., Lehman, W., J Mol Biol 273 (1997) 150–159 .CrossRefGoogle Scholar
[6]Lorenz, M., Popp, D., Holmes, K.C., J Mol Biol 234 (1993) 826–836 .CrossRefGoogle Scholar
[7]Matsudaira, P., Mandelkow, E., Renner, W., Hesterberg, L.K., Weber, K., Nature 301 (1983) 209–214 .CrossRefGoogle Scholar