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Structure paper

TitleThe phosphorylation and dephosphorylation switch of VCP/p97 regulates the architecture of centrosome and spindle.
Journal, issue, pagesCell Death Differ, Vol. 29, Issue 10, Page 2070-2088, Year 2022
Publish dateApr 16, 2022
AuthorsKaiyuan Zhu / Yang Cai / Xiaotong Si / Zuodong Ye / Yuanzhu Gao / Chuang Liu / Rui Wang / Zhibin Ma / Huazhang Zhu / Liang Zhang / Shengjin Li / Hongmin Zhang / Jianbo Yue /
PubMed AbstractThe proper orientation of centrosome and spindle is essential for genome stability; however, the mechanism that governs these processes remains elusive. Here, we demonstrated that polo-like kinase 1 ...The proper orientation of centrosome and spindle is essential for genome stability; however, the mechanism that governs these processes remains elusive. Here, we demonstrated that polo-like kinase 1 (Plk1), a key mitotic kinase, phosphorylates residue Thr76 in VCP/p97 (an AAA-ATPase), at the centrosome from prophase to anaphase. This phosphorylation process recruits VCP to the centrosome and in this way, it regulates centrosome orientation. VCP exhibits strong co-localization with Eg5 (a mitotic kinesin motor), at the mitotic spindle, and the dephosphorylation of Thr76 in VCP is required for the enrichment of both VCP and Eg5 at the spindle, thus ensuring proper spindle architecture and chromosome segregation. We also showed that the phosphatase, PTEN, is responsible for the dephosphorylation of Thr76 in VCP; when PTEN was knocked down, the normal spread of VCP from the centrosome to the spindle was abolished. Cryo-EM structures of VCP and VCP, which represent dephosphorylated and phosphorylated states of VCP, respectively, revealed that the Thr76 phosphorylation modulates VCP by altering the inter-domain and inter-subunit interactions, and ultimately the nucleotide-binding pocket conformation. Interestingly, the tumor growth in nude mice implanted with VCP-reconstituted cancer cells was significantly slower when compared with those implanted with VCP-reconstituted cancer cells. Collectively, our findings demonstrate that the phosphorylation and dephosphorylation switch of VCP regulates the architecture of centrosome and spindle for faithful chromosome segregation.
External linksCell Death Differ / PubMed:35430615 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 4.8 Å
Structure data

30147

7bp8

EMDB-30147, PDB-7bp8:
Human AAA+ ATPase VCP mutant - T76A, ADP-bound form
Method: EM (single particle) / Resolution: 3.9 Å

30148

7bp9

EMDB-30148, PDB-7bp9:
Human AAA+ ATPase VCP mutant - T76E, ADP-bound form
Method: EM (single particle) / Resolution: 3.6 Å

30149

7bpa

EMDB-30149, PDB-7bpa:
Human AAA+ ATPase VCP mutant - T76A, AMP-PNP-bound form, Conformation I
Method: EM (single particle) / Resolution: 3.3 Å

30150

7bpb

EMDB-30150, PDB-7bpb:
Human AAA+ ATPase VCP mutant - T76E, AMP-PNP bound form, Conformation I
Method: EM (single particle) / Resolution: 4.3 Å

EMDB-30153:
Human AAA+ ATPase VCP mutant - T76A, AMP-PNP-bound form, Conformation II
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-30154:
Human AAA+ ATPase VCP mutant - T76E, AMP-PNP-bound form, Conformation II
Method: EM (single particle) / Resolution: 4.8 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • homo sapiens (human)
KeywordsCELL CYCLE / Complex / ATPase / Unfoldase / Protein Transportation

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