Isolation and MS characterisation of recombinant human septin octameric complexes containing distinct SEPT9 isoforms
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive Plus
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: 
Luc Camoin
LAB HEAD: Marseille Proteomics
PROVIDER: PXD023857 | Pride | 2021-07-27
REPOSITORIES: Pride
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Project description:Experimentally deciphering and understanding the interaction network of a particular protein provides often evidence for so far unknown functions. For the septins, a class of cytoskeletal proteins, targeted high-throughput approaches that aim at systematically deciphering interaction partners have not yet been performed. Septins regulate the organization of the acin cytoskeleton, vesicle transport and fusion, chromosome alignment- and segregation, and cytokinesis. SEPT9 is part of the core septin hetero-octamer in human cells which is composed of SEPT2, SEPT6, SEPT7, and SEPT9. SEPT9 has been linked to a variety of intracellular functions as well as to diseases and diverse types of cancer. We applied a quantitative proteomics approach to establish an interactome of SEPT9 in human fibroblast cells. We identified among others so far unknown interaction partners from the myosin familiy and could provide evidence that SEPT9 participates in vesicle transport from and to the plasma membrane as well as in the attachment of actin stress fibers to cellular adhesions.
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