A self-propelled biological process

Park, Jung‐Eun; Erikson, Raymond L.; Lee, Kyung S.

doi:10.4161/cc.10.20.17522

Cited by 2 publications

(2 citation statements)

References 11 publications

(11 reference statements)

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“…In early mitosis, PLK1 induces PBIP1 degradation; however, PLK1 is retained at the kinetochores even after degradation of PBIP1. Thus, the PLK1 population freed from the PBIP1–PLK1 complex must interact with other interacting partners to maintain its position at the kinetochores 36 37 38 . Other kinetochore/centromere-associated proteins, such as Bub1 kinase 28 and INCENP 39 , contribute to PLK1 localization at kinetochores.…”

Section: Discussionmentioning

confidence: 99%

The chromatin remodeller RSF1 is essential for PLK1 deposition and function at mitotic kinetochores

et al. 2015

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Accumulation of PLK1 at kinetochores is essential for chromosome alignment and segregation; however, the mechanism underlying PLK1 recruitment to kinetochores remains unresolved. The chromatin remodeller RSF1 tightly associates with centromere proteins, but its mitotic function is unknown. Here we show that RSF1 localizes at mitotic kinetochores and directly binds PLK1. RSF1 depletion disrupts localization of PLK1 at kinetochores; the C-terminal fragment of RSF1, which can bind PLK1, is sufficient to restore PLK1 localization. Moreover, CDK1 phosphorylates RSF1 at Ser1375, and this phosphorylation is necessary for PLK1 recruitment. Subsequently, PLK1 phosphorylates RSF1 at Ser1359, stabilizing PLK1 deposition. Importantly, RSF1 depletion mimicks the chromosome misalignment phenotype resulting from PLK1 knockdown; these defects are rescued by RSF1 S1375D or RSF1 S1359D but not RSF1 S1375A, showing a functional link between phosphorylation of RSF1 and chromosome alignment. Together, these data show that RSF1 is an essential centromeric component that recruits PLK1 to kinetochores and plays a crucial role in faithful cell division.

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Section: Discussionmentioning

confidence: 99%

The chromatin remodeller RSF1 is essential for PLK1 deposition and function at mitotic kinetochores

et al. 2015

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“…The interaction of PLKs with substrates is reportedly strongly dependent on PLK binding site phosphorylation status [ 29 ]. Nonetheless, low affinity binding to non-phosphorylated binding sites, and a few binding sites phosphorylated by PLKs themselves, have been reported [reviewed in 39 ]. To determine the phosphorylation-status of the putative PFV Gag PLK STP binding site, we examined particle-associated Gag or protein immunoprecipitated from cell lysates with various phosphopeptide-specific antibodies, including a custom-made antiserum specific for the PFV Gag STP motif ( Fig 4 ).…”

Section: Resultsmentioning

confidence: 99%

Interactions of Prototype Foamy Virus Capsids with Host Cell Polo-Like Kinases Are Important for Efficient Viral DNA Integration

et al. 2016

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Unlike for other retroviruses, only a few host cell factors that aid the replication of foamy viruses (FVs) via interaction with viral structural components are known. Using a yeast-two-hybrid (Y2H) screen with prototype FV (PFV) Gag protein as bait we identified human polo-like kinase 2 (hPLK2), a member of cell cycle regulatory kinases, as a new interactor of PFV capsids. Further Y2H studies confirmed interaction of PFV Gag with several PLKs of both human and rat origin. A consensus Ser-Thr/Ser-Pro (S-T/S-P) motif in Gag, which is conserved among primate FVs and phosphorylated in PFV virions, was essential for recognition by PLKs. In the case of rat PLK2, functional kinase and polo-box domains were required for interaction with PFV Gag. Fluorescently-tagged PFV Gag, through its chromatin tethering function, selectively relocalized ectopically expressed eGFP-tagged PLK proteins to mitotic chromosomes in a Gag STP motif-dependent manner, confirming a specific and dominant nature of the Gag-PLK interaction in mammalian cells. The functional relevance of the Gag-PLK interaction was examined in the context of replication-competent FVs and single-round PFV vectors. Although STP motif mutated viruses displayed wild type (wt) particle release, RNA packaging and intra-particle reverse transcription, their replication capacity was decreased 3-fold in single-cycle infections, and up to 20-fold in spreading infections over an extended time period. Strikingly similar defects were observed when cells infected with single-round wt Gag PFV vectors were treated with a pan PLK inhibitor. Analysis of entry kinetics of the mutant viruses indicated a post-fusion defect resulting in delayed and reduced integration, which was accompanied with an enhanced preference to integrate into heterochromatin. We conclude that interaction between PFV Gag and cellular PLK proteins is important for early replication steps of PFV within host cells.

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A self-propelled biological process

Cited by 2 publications

References 11 publications

The chromatin remodeller RSF1 is essential for PLK1 deposition and function at mitotic kinetochores

The chromatin remodeller RSF1 is essential for PLK1 deposition and function at mitotic kinetochores

Interactions of Prototype Foamy Virus Capsids with Host Cell Polo-Like Kinases Are Important for Efficient Viral DNA Integration

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