Linked Life Data

15817481

Source:http://linkedlifedata.com/resource/pubmed/id/15817481

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
2005-6-6
pubmed:abstractText
The binding of plectin to the beta4 subunit of the alpha6beta4 integrin is a critical step in the formation of hemidesmosomes. An important interaction between these two proteins occurs between the actin-binding domain (ABD) of plectin and the first pair of fibronectin type III (FNIII) domains and a small part of the connecting segment of beta4. Previously, a few amino acids, critical for this interaction, were identified in both plectin and beta4 and mapped on the crystal structures of the ABD of plectin and the first pair of FNIII domains of beta4. In the present study, we used this biochemical information and protein-protein docking calculations to construct a model of the binary complex between these two protein domains. The top scoring computational model predicts that the calponin-homology 1 (CH1) domain of the ABD associates with the first and the second FNIII domains of beta4. Our mutational analysis of the residues at the proposed interface of both the FNIII and the CH1 domains is in agreement with the suggested interaction model. Computational simulations to predict protein motions suggest that the exact model of FNIII and plectin CH1 interaction might well differ in detail from the suggested model due to the conformational plasticity of the FNIII domains, which might lead to a closely related but different mode of interaction with the plectin-ABD. Furthermore, we show that Ser-1325 in the connecting segment of beta4 appears to be essential for the recruitment of plectin into hemidesmosomes in vivo. This is consistent with the proposed model and previously published mutational data. In conclusion, our data support a model in which the CH1 domain of the plectin-ABD associates with the groove between the two FNIII domains of beta4.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
22270-7
pubmed:dateRevised
2011-10-27
pubmed:meshHeading
pubmed-meshheading:15817481-Actins, pubmed-meshheading:15817481-Animals, pubmed-meshheading:15817481-Binding Sites, pubmed-meshheading:15817481-COS Cells, pubmed-meshheading:15817481-Cell Line, pubmed-meshheading:15817481-DNA, Complementary, pubmed-meshheading:15817481-Fibronectins, pubmed-meshheading:15817481-Humans, pubmed-meshheading:15817481-Immunoblotting, pubmed-meshheading:15817481-Integrin beta4, pubmed-meshheading:15817481-Intermediate Filament Proteins, pubmed-meshheading:15817481-Macromolecular Substances, pubmed-meshheading:15817481-Models, Molecular, pubmed-meshheading:15817481-Mutation, pubmed-meshheading:15817481-Peptide Mapping, pubmed-meshheading:15817481-Phosphorylation, pubmed-meshheading:15817481-Plectin, pubmed-meshheading:15817481-Protein Binding, pubmed-meshheading:15817481-Protein Conformation, pubmed-meshheading:15817481-Protein Structure, Tertiary, pubmed-meshheading:15817481-Proteins, pubmed-meshheading:15817481-Recombinant Fusion Proteins, pubmed-meshheading:15817481-Serine, pubmed-meshheading:15817481-Software, pubmed-meshheading:15817481-Two-Hybrid System Techniques
pubmed:year
2005
pubmed:articleTitle
Modeling and experimental validation of the binary complex of the plectin actin-binding domain and the first pair of fibronectin type III (FNIII) domains of the beta4 integrin.
pubmed:affiliation
Divisions of Cell Biology, and Molecular Carcinogenesis, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't