JBC Oz Biosciences

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Shi, J.
Right arrow Articles by Sugrue, S. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shi, J.
Right arrow Articles by Sugrue, S. P.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 275, Issue 20, 14910-14915, May 19, 2000

Dissection of Protein Linkage between Keratins and Pinin, a Protein with Dual Location at Desmosome-Intermediate Filament Complex and in the Nucleus*

Jia Shi and Stephen P. SugrueDagger

From the Department of Anatomy and Cell Biology, University of Florida College of Medicine, Gainesville, Florida 32610-0235

Pinin is a cell adhesion-associated and nuclear protein that has been shown to localize in the vicinity of intermediate filament (IF) convergence upon the cytoplasmic face of the desmosomal plaque as well as in the nucleus. The localization of pinin to the desmosomes has been correlated with the reinforcement of intercellular adhesion and increased IF organization. In this study, keratins 18, 8, and 19 were identified to interact with the amino end domain of pinin in a two-hybrid screening. Further truncation analyses indicated that the 2B domain of keratin contains the sequence responsible for interacting with pinin. The amino end of pinin (residues 1-98) is sufficient to bind to keratin. Point mutation analyses revealed two essential residues within the pinin fragment 1-98, leucine 8 and leucine 19, for the interaction with keratin. Finally, in vitro protein overlay binding assays confirmed the direct interaction of the amino end domain of pinin with keratins, while pinin mutant L8P GST fusion protein failed to bind to keratins in the overlay assay. Coupled with our previous morphological observations and transfection studies, these data suggest that pinin may play a role in epithelial cell adhesion and the IF complex through a direct interaction with the keratin filaments.


* This work was supported by National Institutes of Health Grant EY07883.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Anatomy and Cell Biology, University of Florida College of Medicine, 1600 S.W. Archer Rd., Gainesville, FL 32610-0235. Tel.: 352-392-3569; Fax: 352-392-3305; E-mail: sugrue@anatomy.med.ufl.edu.


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Mol. Cell. Biol.Home page
R. Alpatov, Y. Shi, G. C. Munguba, B. Moghimi, J.-H. Joo, J. Bungert, and S. P. Sugrue
Corepressor CtBP and Nuclear Speckle Protein Pnn/DRS Differentially Modulate Transcription and Splicing of the E-Cadherin Gene
Mol. Cell. Biol., March 1, 2008; 28(5): 1584 - 1595.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
R. Alpatov, G. C. Munguba, P. Caton, J. H. Joo, Y. Shi, Y. Shi, M. E. Hunt, and S. P. Sugrue
Nuclear Speckle-Associated Protein Pnn/DRS Binds to the Transcriptional Corepressor CtBP and Relieves CtBP- Mediated Repression of the E-Cadherin Gene
Mol. Cell. Biol., December 1, 2004; 24(23): 10223 - 10235.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
K. E. Rieger and G. Chu
Portrait of transcriptional responses to ultraviolet and ionizing radiation in human cells
Nucleic Acids Res., September 8, 2004; 32(16): 4786 - 4803.
[Abstract] [Full Text] [PDF]


Home page
IOVSHome page
G. Zimowska, J. Shi, G. Munguba, M. R. Jackson, R. Alpatov, M. N. Simmons, Y. Shi, and S. P. Sugrue
Pinin/DRS/memA Interacts with SRp75, SRm300 and SRrp130 in Corneal Epithelial Cells
Invest. Ophthalmol. Vis. Sci., November 1, 2003; 44(11): 4715 - 4723.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. S. Kedar, S.-J. Kim, A. Robertson, E. Hou, R. Prasad, J. K. Horton, and S. H. Wilson
Direct Interaction between Mammalian DNA Polymerase beta and Proliferating Cell Nuclear Antigen
J. Biol. Chem., August 16, 2002; 277(34): 31115 - 31123.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.