GTP Binding Is Required for SEPT12 to Form Filaments and to Interact with SEPT11

다국어 초록 (Multilingual Abstract)

Septins are a family of filament-forming GTP-binding
proteins involved in a variety of cellular process such
as cytokinesis, exocytosis, and membrane dynamics.
Here we report the biochemical and immunocytochemical
characterization of a recently identified
mammalian septin, SEPT12. SEPT12 binds GTP in
vitro, and a mutation (Gly56 to Asn) in the GTPbinding
motif abolished binding. Immunocytochemical
analysis revealed that wild-type SEPT12 formed filamentous
structures when transiently expressed in Hela
cells whereas SEPT12G56A generated large aggregates.
In addition, wild-type SEPT12 failed to form filaments
when coexpressed with SEPT12G56A. We also observed
that GTP-binding by SEPT12 is required for interaction
with SEPT11 but not with itself.

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