Septin

Cell division/GTP binding protein
Identifiers
SymbolCell_Div_GTP_bd
PfamPF00735
Pfam clanCL0023
InterProIPR000038
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Septins are a group of GTP-binding proteins expressed in all eukaryotic cells except plants.[1][2][3] Different septins form protein complexes with each other. These complexes can further assemble into filaments, rings and gauzes. Assembled as such, septins function in cells by localizing other proteins, either by providing a scaffold to which proteins can attach, or by forming a barrier preventing the diffusion of molecules from one compartment of the cell to another,[2][3][4][5] or in the cell cortex as a barrier to the diffusion of membrane-bound proteins.[6]

Septins have been implicated in the localization of cellular processes at the site of cell division, and at the cell membrane at sites where specialized structures like cilia or flagella are attached to the cell body.[4] In yeast cells, they compartmentalize parts of the cell and build scaffolding to provide structural support during cell division at the septum, from which they derive their name.[3] Research in human cells suggests that septins build cages around pathogenic bacteria, that immobilize and prevent them from invading other cells.[7]

As filament forming proteins, septins can be considered part of the cytoskeleton.[4] Apart from forming non-polar filaments, septins associate with cell membranes, the cell cortex, actin filaments and microtubules.[4][6]

  1. ^ Cite error: The named reference Neubauer was invoked but never defined (see the help page).
  2. ^ a b Weirich CS, Erzberger JP, Barral Y (2008). "The septin family of GTPases: architecture and dynamics". Nat. Rev. Mol. Cell Biol. 9 (6): 478–89. doi:10.1038/nrm2407. PMID 18478031. S2CID 2640351.
  3. ^ a b c Douglas LM, Alvarez FJ, McCreary C, Konopka JB (2005). "Septin function in yeast model systems and pathogenic fungi". Eukaryotic Cell. 4 (9): 1503–12. doi:10.1128/EC.4.9.1503-1512.2005. PMC 1214204. PMID 16151244.
  4. ^ a b c d Mostowy S, Cossart P (2012). "Septins: the fourth component of the cytoskeleton". Nat. Rev. Mol. Cell Biol. 13 (3): 183–94. doi:10.1038/nrm3284. PMID 22314400. S2CID 2418522.
  5. ^ Kinoshita M (2006). "Diversity of septin scaffolds". Curr. Opin. Cell Biol. 18 (1): 54–60. doi:10.1016/j.ceb.2005.12.005. PMID 16356703.
  6. ^ a b Bridges, AA; Gladfelter, AS (10 July 2015). "Septin Form and Function at the Cell Cortex". The Journal of Biological Chemistry. 290 (28): 17173–80. doi:10.1074/jbc.R114.634444. PMC 4498057. PMID 25957401.
  7. ^ Mascarelli A (December 2011). "Septin proteins take bacterial prisoners: A cellular defence against microbial pathogens holds therapeutic potential". Nature. doi:10.1038/nature.2011.9540. S2CID 85080734.