Structures of two intermediate filament-binding fragments of desmoplakin reveal a unique repeat motif structure

Hee Jung Choi; Shaun Park-Snyder; Lauren T. Pascoe; Kathleen J. Green; William I. Weis

doi:10.1038/nsb818

Structures of two intermediate filament-binding fragments of desmoplakin reveal a unique repeat motif structure

Hee Jung Choi, Shaun Park-Snyder, Lauren T. Pascoe, Kathleen J. Green, William I. Weis

Robert H. Lurie Comprehensive Cancer Center

Research output: Contribution to journal › Article › peer-review

100 Scopus citations

Abstract

Desmosomes are intercellular junctions in which cadherin cell adhesion molecules are linked to the intermediate filament (IF) system. Desmoplakin is a member of the plakin family of IF-binding proteins. The C-terminal domain of desmoplakin (DPCT) mediates binding to IFs in desmosomes. The DPCT sequence contains three regions, termed A, B and C, consisting of 4.5 copies of a 38-amino acid repeat motif. We demonstrate that these regions form discrete subdomains that bind to IFs and report the crystal structures of domains B and C. In contrast to the elongated structures formed by other kinds of repeat motifs, the plakin repeats form a globular structure with a unique fold. A conserved basic groove found on the domain may represent an IF-binding site.

Original language	English (US)
Pages (from-to)	612-620
Number of pages	9
Journal	Nature Structural Biology
Volume	9
Issue number	8
DOIs	https://doi.org/10.1038/nsb818
State	Published - 2002

Funding

We thank P. Ellis for beamline support. Portions of this research were carried out at the Stanford Synchrotron Radiation Laboratory (SSRL), a national user facility operated by Stanford University on behalf of the U.S. Department of Energy, Office of Basic Energy Sciences. The SSRL Structural Molecular Biology Program is supported by the Department of Energy, Office of Biological and Environmental Research, and by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program, and the National Institute of General Medical Sciences. H.-J.C. was supported by fellowships from the Korea Science and Engineering Foundation and the American Heart Association. This work was supported by grants to W.I.W. and K.J.G from the National Institutes of Health.

ASJC Scopus subject areas

Genetics
Structural Biology
Biochemistry

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title = "Structures of two intermediate filament-binding fragments of desmoplakin reveal a unique repeat motif structure",

abstract = "Desmosomes are intercellular junctions in which cadherin cell adhesion molecules are linked to the intermediate filament (IF) system. Desmoplakin is a member of the plakin family of IF-binding proteins. The C-terminal domain of desmoplakin (DPCT) mediates binding to IFs in desmosomes. The DPCT sequence contains three regions, termed A, B and C, consisting of 4.5 copies of a 38-amino acid repeat motif. We demonstrate that these regions form discrete subdomains that bind to IFs and report the crystal structures of domains B and C. In contrast to the elongated structures formed by other kinds of repeat motifs, the plakin repeats form a globular structure with a unique fold. A conserved basic groove found on the domain may represent an IF-binding site.",

author = "Choi, {Hee Jung} and Shaun Park-Snyder and Pascoe, {Lauren T.} and Green, {Kathleen J.} and Weis, {William I.}",

note = "Funding Information: We thank P. Ellis for beamline support. Portions of this research were carried out at the Stanford Synchrotron Radiation Laboratory (SSRL), a national user facility operated by Stanford University on behalf of the U.S. Department of Energy, Office of Basic Energy Sciences. The SSRL Structural Molecular Biology Program is supported by the Department of Energy, Office of Biological and Environmental Research, and by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program, and the National Institute of General Medical Sciences. H.-J.C. was supported by fellowships from the Korea Science and Engineering Foundation and the American Heart Association. This work was supported by grants to W.I.W. and K.J.G from the National Institutes of Health.",

year = "2002",

doi = "10.1038/nsb818",

language = "English (US)",

volume = "9",

pages = "612--620",

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AU - Park-Snyder, Shaun

AU - Pascoe, Lauren T.

AU - Green, Kathleen J.

AU - Weis, William I.

N1 - Funding Information: We thank P. Ellis for beamline support. Portions of this research were carried out at the Stanford Synchrotron Radiation Laboratory (SSRL), a national user facility operated by Stanford University on behalf of the U.S. Department of Energy, Office of Basic Energy Sciences. The SSRL Structural Molecular Biology Program is supported by the Department of Energy, Office of Biological and Environmental Research, and by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program, and the National Institute of General Medical Sciences. H.-J.C. was supported by fellowships from the Korea Science and Engineering Foundation and the American Heart Association. This work was supported by grants to W.I.W. and K.J.G from the National Institutes of Health.

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N2 - Desmosomes are intercellular junctions in which cadherin cell adhesion molecules are linked to the intermediate filament (IF) system. Desmoplakin is a member of the plakin family of IF-binding proteins. The C-terminal domain of desmoplakin (DPCT) mediates binding to IFs in desmosomes. The DPCT sequence contains three regions, termed A, B and C, consisting of 4.5 copies of a 38-amino acid repeat motif. We demonstrate that these regions form discrete subdomains that bind to IFs and report the crystal structures of domains B and C. In contrast to the elongated structures formed by other kinds of repeat motifs, the plakin repeats form a globular structure with a unique fold. A conserved basic groove found on the domain may represent an IF-binding site.

AB - Desmosomes are intercellular junctions in which cadherin cell adhesion molecules are linked to the intermediate filament (IF) system. Desmoplakin is a member of the plakin family of IF-binding proteins. The C-terminal domain of desmoplakin (DPCT) mediates binding to IFs in desmosomes. The DPCT sequence contains three regions, termed A, B and C, consisting of 4.5 copies of a 38-amino acid repeat motif. We demonstrate that these regions form discrete subdomains that bind to IFs and report the crystal structures of domains B and C. In contrast to the elongated structures formed by other kinds of repeat motifs, the plakin repeats form a globular structure with a unique fold. A conserved basic groove found on the domain may represent an IF-binding site.

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Structures of two intermediate filament-binding fragments of desmoplakin reveal a unique repeat motif structure

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