SEPT12 interacts with SEPT6 and this interaction alters the filament structure of SEPT6 in Hela cells.
Septins are a family of conserved cytoskeletal GTPase forming heteropolymeric filamentous structure in interphase cells, however, the mechanism of assembly are largely unknown. Here we described the characterization of SEPT12, sharing closest homology to SEPT3 and SEPT9. It was revealed that subcellular localization of SEPT12 varied at interphase and mitotic phase. While SEPT12 formed filamentous structures at interphase, it was localized to the central spindle and to midbody during anaphase and cytokinesis, respectively. In addition, we found that SEPT12 can interact with SEPT6 in vitro and in vivo, and this interaction was independent of the coiled coil domain of SEPT6. Further, co-expression of SEPT12 altered the filamentous structure of SEPT6 in Hela cells. Therefore, our result showed that the interaction between different septins may affect the septin filament structure.
State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Science, Fudan University, Shanghai 200433, PR China.
Xiangming
X
Ding
Wenbo
W
Yu
Ming
M
Liu
Suqin
S
Shen
Fang
F
Chen
Bo
B
Wan
Long
L
Yu
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D003598:Cytoskeletal Proteins; D017931:DNA Primers / Q000235:genetics; D019204:GTP-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D007399:Interphase; D008938:Mitosis; D008969:Molecular Sequence Data; D010802:Phylogeny; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D058112:Septins; D017386:Sequence Homology, Amino Acid; D013347:Subcellular Fractions / Q000378:metabolism
D003598:Cytoskeletal Proteins; D017931:DNA Primers; D011994:Recombinant Proteins; D019204:GTP-Binding Proteins; C502729:SEPTIN12 protein, human; C436485:SEPTIN6 protein, human; D058112:Septins