The novel human platelet septin SEPT8 is an interaction partner of SEPT4.

Septins are a family of GTP-binding proteins, which are essential for active membrane movement such as cytokinesis and vesicle trafficking. In non-dividing cells (such as platelets and neurons) septins are implicated in exocytosis. Platelets from a SEPT5 knockout mouse showed an altered serotonin secretion and platelet aggregation, suggesting that SEPT5 is involved in secretion in platelets.

Isolation of new splice isoforms, characterization and expression analysis of the human septin SEPT8 (KIAA0202).

SEPT8 (KIAA0202) is a member of the highly conserved septin family. Septins are membrane-associated GTPases which are involved in cytokinesis and cellular morphogenesis. Using the yeast two-hybrid system and the glutathione-S-transferase pull-down assay we previously had identified the SEPT8 (KIAA0202) as interaction partner of the human septin SEPT5 (cell division cycle related-1, CDCrel-1).

Human septin-septin interaction: CDCrel-1 partners with KIAA0202.

Septins are evolutionary conserved cytoskeletal GTPases forming heteropolymer complexes involved in cytokinesis and other cellular processes. CDCrel-1 (cell division cycle related-1) is a recently cloned and characterized human septin which is highly expressed in non-dividing cells, such as neurons. Using a yeast two-hybrid system we demonstrate that CDCrel-1 partners with another uncharacterized human septin, KIAA0202.