J. Biochem, 2003, Vol. 134, No. 4 491-496
© 2003 Japanese Biochemical Society
JB MINIREVIEWS |
Assembly of Mammalian Septins
1 Biochemistry and Cell Biology Unit, HMRO, Kyoto University Graduate School of Medicine; and 2 PRESTO, Japan Science and Technology Agency, Yoshida Konoe, Sakyo, Kyoto 606-8501
ABSTRACT
Septins are a conserved family of polymerizing guanine nucleotide binding proteins associated with diverse processes in dividing and non-dividing cells. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Native and recombinant mammalian septin complexes are purified as ~8-nm-thick filaments of variable length. Ultrastructurally, a mammalian septin filament appears an irregular array of structural segments, whose polarity is obscure. The filaments have a potential to self-assemble into higher-order structures by lateral stacking and tandem annealing, eventually forming uniformly curved bundles, i.e., rings and coils. The septin filaments also undergo templated assembly along existing actin bundles containing an adapter protein, anillin. The resultant higher-order assembly of septin filaments may provide scaffolds to recruit other molecules and/or help organize the actin-based structures. The in vitro self-assembly is an irreversible process, which is not coupled with robust nucleotide exchange or hydrolysis. In contrast, septin-based structures rearrange and disassemble in cells, which might be controlled by diverse factors (e.g., the Cdc42-borg system, anillin, syntaxin, phospholipids) and covalent modifications (e.g., phosphorylation, ubiquitination, sumoylation). An immediate goal of septin biochemistry is to define the mechanisms of assembly and disassembly of this elusive cytoskeleton.
FOOTNOTES
* To whom correspondence should be addressed. Tel: +81-75-753-9298, Fax: +81-75-753-9311, E-mail: mkinoshita{at}hmro.med.kyoto-u.ac.jp
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  M. Zhu, F. Wang, F. Yan, P. Y. Yao, J. Du, X. Gao, X. Wang, Q. Wu, T. Ward, J. Li, et al. Septin 7 Interacts with Centromere-associated Protein E and Is Required for Its Kinetochore Localization J. Biol. Chem., July 4, 2008; 283(27): 18916 - 18925. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 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]
|
|
|
|
 |
|
 C. S. Kim, S. K. Seol, O.-K. Song, J. H. Park, and S. K. Jang An RNA-Binding Protein, hnRNP A1, and a Scaffold Protein, Septin 6, Facilitate Hepatitis C Virus Replication J. Virol., April 15, 2007; 81(8): 3852 - 3865. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 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]
|
|
|
|
 |
|
 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]
|
|
|
|
 |
|
 A. N. Gillis, S. Thomas, S. D. Hansen, and K. B. Kaplan A novel role for the CBF3 kinetochore-scaffold complex in regulating septin dynamics and cytokinesis J. Cell Biol., December 5, 2005; 171(5): 773 - 784. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. M. Douglas, F. J. Alvarez, C. McCreary, and J. B. Konopka Septin Function in Yeast Model Systems and Pathogenic Fungi Eukaryot. Cell, September 1, 2005; 4(9): 1503 - 1512. [Full Text] [PDF]
|
|
|
|
|
|
M. Pache, B. Zieger, S. Blaser, and P. Meyer Immunoreactivity of the Septins SEPT4, SEPT5, and SEPT8 in the Human Eye J. Histochem. Cytochem., September 1, 2005; 53(9): 1139 - 1147. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K.-i. Nagata, T. Asano, Y. Nozawa, and M. Inagaki Biochemical and Cell Biological Analyses of a Mammalian Septin Complex, Sept7/9b/11 J. Biol. Chem., December 31, 2004; 279(53): 55895 - 55904. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Martinez and J. Ware Mammalian Septin Function in Hemostasis and Beyond Experimental Biology and Medicine, December 1, 2004; 229(11): 1111 - 1119. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. Kato, C. Martinez, S. Russell, P. Nurden, A. Nurden, S. Fiering, and J. Ware Genetic deletion of mouse platelet glycoprotein Ib{beta} produces a Bernard-Soulier phenotype with increased {alpha}-granule size Blood, October 15, 2004; 104(8): 2339 - 2344. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Dobbelaere and Y. Barral Spatial Coordination of Cytokinetic Events by Compartmentalization of the Cell Cortex Science, July 16, 2004; 305(5682): 393 - 396. [Abstract] [Full Text] [PDF]
|
|