Advertisement
JBC

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


     


Originally published In Press as doi:10.1074/jbc.M406153200 on October 12, 2004

J. Biol. Chem., Vol. 279, Issue 53, 55895-55904, December 31, 2004
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
279/53/55895    most recent
M406153200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nagata, K.-i.
Right arrow Articles by Inagaki, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nagata, K.-i.
Right arrow Articles by Inagaki, M.
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?

Biochemical and Cell Biological Analyses of a Mammalian Septin Complex, Sept7/9b/11*

Koh-ichi Nagata{ddagger}§, Tomiko Asano{ddagger}, Yoshinori Nozawa||, and Masaki Inagaki§

From the {ddagger}Department of Molecular Neurobiology, the Institute for Developmental Research, Aichi Human Service Center, 713-8 Kamiya-Cho, Kasugai, Aichi 480-0392, Japan, the §Division of Biochemistry, Aichi Cancer Center Research Institute, 1-1 Kanokoden, Chikusa, Nagoya 464-8681, ||Gifu International Institute of Biotechnology, 1-1 Nakafudogaoka, Gifu 504-0838, Japan

Septins are members of a conserved family of cytoskeletal GTPases present in organisms as diverse as yeast and mammals. Unlike lower eukaryotic cells, the physiological significance of mammalian septin complexes is largely unknown. Using specific antibodies, we found at least five septins, Sept2, Sept7, Sept8, Sept9b, and Sept11, in septin complexes affinity-purified with anti-Sept7 antibody-conjugated column from rat embryonic fibroblast REF52 cells. Immunofluorescence studies revealed co-localization of Sept7, Sept9b, and Sept11 along stress fibers in REF52 cells. Biochemical and immunoprecipitation analyses revealed that the three septins directly bind with each other through their N- or C-terminal divergent regions. These septins per se formed distinct and characteristic filament structures when transiently expressed in COS7 cells. When two of the three septins were co-expressed in COS7 cells, combination-dependent filament elongation, bundling, or disruption was observed. Taken together, our results suggest that septin filament structures may be affected by interactions with other septins included in the complex.


Received for publication, June 2, 2004 , and in revised form, October 7, 2004.

* This work was supported by grants-in-aid for scientific research and for cancer research from the Ministry of Education, Science, Technology, Sports, and Culture of Japan, by a grant-in-aid for the Second Term Comprehensive 10-Year Strategy for Cancer Control from the Ministry of Health, Labour, and Welfare, Japan, and by a grant from Yamanouchi Foundation for Research on Metabolic Disorders. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Molecular Neurobiology, The Institute for Developmental Research, Aichi Human Service Center, 713-8 Kamiya-Cho, Kasugai, Aichi 480-0392, Japan. Tel.: 81-568-88-0811 (ext. 3595); Fax: 81-568-88-0829; E-mail: knagata{at}inst-hsc.jp.


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
X. Li, D. R. Serwanski, C. P. Miralles, K.-i. Nagata, and A. L. De Blas
Septin 11 Is Present in GABAergic Synapses and Plays a Functional Role in the Cytoarchitecture of Neurons and GABAergic Synaptic Connectivity
J. Biol. Chem., June 19, 2009; 284(25): 17253 - 17265.
[Abstract] [Full Text] [PDF]


Home page
NeurologyHome page
M. C. Hannibal, E. K. Ruzzo, L. R. Miller, B. Betz, J. G. Buchan, D. M. Knutzen, K. Barnett, M. L. Landsverk, A. Brice, E. LeGuern, et al.
SEPT9 gene sequencing analysis reveals recurrent mutations in hereditary neuralgic amyotrophy
Neurology, May 19, 2009; 72(20): 1755 - 1759.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Mostowy, A. Danckaert, T. N. Tham, C. Machu, S. Guadagnini, J. Pizarro-Cerda, and P. Cossart
Septin 11 Restricts InlB-mediated Invasion by Listeria
J. Biol. Chem., April 24, 2009; 284(17): 11613 - 11621.
[Abstract] [Full Text] [PDF]


Home page
Hum Mol GenetHome page
M. L. Landsverk, E. K. Ruzzo, H. C. Mefford, K. Buysse, J. G. Buchan, E. E. Eichler, E. M. Petty, E. A. Peterson, D. M. Knutzen, K. Barnett, et al.
Duplication within the SEPT9 gene associated with a founder effect in North American families with hereditary neuralgic amyotrophy
Hum. Mol. Genet., April 1, 2009; 18(7): 1200 - 1208.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
C. W. Tsang, M. Fedchyshyn, J. Harrison, H. Xie, J. Xue, P. J. Robinson, L.-Y. Wang, and W. S. Trimble
Superfluous Role of Mammalian Septins 3 and 5 in Neuronal Development and Synaptic Transmission
Mol. Cell. Biol., December 1, 2008; 28(23): 7012 - 7029.
[Abstract] [Full Text] [PDF]


Home page
J. Histochem. Cytochem.Home page
X. Xin, M. Pache, B. Zieger, I. Bartsch, C. Prunte, J. Flammer, and P. Meyer
Septin Expression in Proliferative Retinal Membranes
J. Histochem. Cytochem., November 1, 2007; 55(11): 1089 - 1094.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C. Low and I. G. Macara
Structural Analysis of Septin 2, 6, and 7 Complexes
J. Biol. Chem., October 13, 2006; 281(41): 30697 - 30706.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
E. T. Spiliotis and W. J. Nelson
Here come the septins: novel polymers that coordinate intracellular functions and organization
J. Cell Sci., January 1, 2006; 119(1): 4 - 10.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
R. Ono, M. Ihara, H. Nakajima, K. Ozaki, Y. Kataoka-Fujiwara, T. Taki, K.-i. Nagata, M. Inagaki, N. Yoshida, T. Kitamura, et al.
Disruption of Sept6, a Fusion Partner Gene of MLL, Does Not Affect Ontogeny, Leukemogenesis Induced by MLL-SEPT6, or Phenotype Induced by the Loss of Sept4
Mol. Cell. Biol., December 15, 2005; 25(24): 10965 - 10978.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
B. E. Kremer, T. Haystead, and I. G. Macara
Mammalian Septins Regulate Microtubule Stability through Interaction with the Microtubule-binding Protein MAP4
Mol. Biol. Cell, October 1, 2005; 16(10): 4648 - 4659.
[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 © 2004 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement