期刊
JOURNAL OF CELL BIOLOGY
卷 220, 期 3, 页码 -出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.202004196
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- Deutsche Forschungsgemeinschaft [Schi 295/5-3]
This study reveals the initial steps of SPB assembly in yeast, including the interaction between N-Sfi1 and SPB components, as well as a new function of Cdc31 in recruiting dSPB components. These findings provide important insights into our understanding of SPB assembly.
The spindle pole body (SPB) provides microtubule-organizing functions in yeast and duplicates exactly once per cell cycle. The first step in SPB duplication is the half-bridge to bridge conversion via the antiparallel dimerization of the centrin (Cdc31)-binding protein Sfi1 in anaphase. The bridge, which is anchored to the old SPB on the proximal end, exposes free Sfi1 N-termini (N-Sfi1) at its distal end. These free N-Sfi1 promote in G(1) the assembly of the daughter SPB (dSPB) in a yet unclear manner. This study shows that N-Sfi1 including the first three Cdc31 binding sites interacts with the SPB components Spc29 and Spc42, triggering the assembly of the dSPB. Cdc31 binding to N-Sfi1 promotes Spc29 recruitment and is essential for satellite formation. Furthermore, phosphorylation of N-Sfi1 has an inhibitory effect and delays dSPB biogenesis until G(1). Taking these data together, we provide an understanding of the initial steps in SPB assembly and describe a new function of Cdc31 in the recruitment of dSPB components.
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