JBC INTERFERin siRNA transfection reagent

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 QUICK SEARCH:   [advanced]


     


A more recent version of this article appeared on March 15, 2002
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
277/12/10332    most recent
M109979200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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 Shimizu, T.
Right arrow Articles by Hakoshima, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shimizu, T.
Right arrow Articles by Hakoshima, T.
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?

Papers In Press, published online ahead of print December 27, 2001
J. Biol. Chem, 10.1074/jbc.M109979200
Submitted on October 16, 2001
Revised on December 14, 2001
Accepted on December 27, 2001

Structural basis for neurofibromatosis type 2: Crystal structure of the merlin FERM domain

Toshiyuki Shimizu, Azusa Seto, Nobuo Maita, Keisuke Hamada, Shoichiro Tsukita, Sachiko Tsukita, and Toshio Hakoshima

Yokohama City University, Yokohama 230-0045

Corresponding Author: shimizu{at}tsurumi.yokohama-cu.ac.jp

Neurofibromatosis type 2 (NF2) is a dominantly inherited disease associated with the central nervous system. The NF2 gene product merlin is a tumor suppressor and its mutation or inactivation causes this disease. We report here the crystal structure of the merlin FERM domain containing a 22-residue a-helical segment. The structure reveals that the merlin FERM domain consists of three subdomains displaying notable features of the electrostatic surface potentials, although the overall surface potentials similar to those of ezrin/radixin/moesin (ERM) proteins indicate its electrostatic membrane association. The structure also suggests the inactivation mechanisms caused by the pathogenic mutations associated with NF2.


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
J. Biol. Chem.Home page
T. Mori, K. Kitano, S.-i. Terawaki, R. Maesaki, Y. Fukami, and T. Hakoshima
Structural Basis for CD44 Recognition by ERM Proteins
J. Biol. Chem., October 24, 2008; 283(43): 29602 - 29612.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
B. K. Cole, M. Curto, A. W. Chan, and A. I. McClatchey
Localization to the Cortical Cytoskeleton Is Necessary for Nf2/Merlin-Dependent Epidermal Growth Factor Receptor Silencing
Mol. Cell. Biol., February 15, 2008; 28(4): 1274 - 1284.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. F. J. Ceccarelli, H. K. Song, F. Poy, M. D. Schaller, and M. J. Eck
Crystal Structure of the FERM Domain of Focal Adhesion Kinase
J. Biol. Chem., January 6, 2006; 281(1): 252 - 259.
[Abstract] [Full Text] [PDF]


Home page
Genes Dev.Home page
A. I. McClatchey and M. Giovannini
Membrane organization and tumorigenesis--the NF2 tumor suppressor, Merlin
Genes & Dev., October 1, 2005; 19(19): 2265 - 2277.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
J. M. Dunty, V. Gabarra-Niecko, M. L. King, D. F. J. Ceccarelli, M. J. Eck, and M. D. Schaller
FERM Domain Interaction Promotes FAK Signaling
Mol. Cell. Biol., June 15, 2004; 24(12): 5353 - 5368.
[Abstract] [Full Text] [PDF]


Home page
Sci SignalHome page
J. P. DiNitto, T. C. Cronin, and D. G. Lambright
Membrane Recognition and Targeting by Lipid-Binding Domains
Sci. Signal., December 16, 2003; 2003(213): re16 - re16.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Gautreau, B. T. Fievet, E. Brault, C. Antony, A. Houdusse, D. Louvard, and M. Arpin
Isolation and Characterization of an Aggresome Determinant in the NF2 Tumor Suppressor
J. Biol. Chem., February 14, 2003; 278(8): 6235 - 6242.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
W. J. Smith, N. Nassar, A. Bretscher, R. A. Cerione, and P. A. Karplus
Structure of the Active N-terminal Domain of Ezrin. CONFORMATIONAL AND MOBILITY CHANGES IDENTIFY KEYSTONE INTERACTIONS
J. Biol. Chem., February 7, 2003; 278(7): 4949 - 4956.
[Abstract] [Full Text] [PDF]


Home page
Hum Mol GenetHome page
M. Kressel and B. Schmucker
Nucleocytoplasmic transfer of the NF2 tumor suppressor protein merlin is regulated by exon 2 and a CRM1-dependent nuclear export signal in exon 15
Hum. Mol. Genet., September 15, 2002; 11(19): 2269 - 2278.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
C.-X. Sun, V. A. Robb, and D. H. Gutmann
Protein 4.1 tumor suppressors: getting a FERM grip on growth regulation
J. Cell Sci., January 11, 2002; 115(21): 3991 - 4000.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.