Bicaudal D2, Dynein, and Kinesin-1 Associate with Nuclear Pore Complexes and Regulate Centrosome and Nuclear Positioning during Mitotic Entry

Splinter, Daniël; Tanenbaum, Marvin E.; Lindqvist, Arne; Jaarsma, Dick; Flotho, Annette; Yu, Ka Lou; Grigoriev, Ilya; Engelsma, Dieuwke; Haasdijk, Elize D.; Keijzer, Nanda; Demmers, Jeroen; Fornerod, Maarten; Melchior, Frauke; Hoogenraad, Casper C.; Medema, René H.; Akhmanova, Anna

doi:10.1371/journal.pbio.1000350

Cited by 287 publications

(468 citation statements)

References 67 publications

(125 reference statements)

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“…The same study (Splinter et al, 2010) also indicated that Kinesin1, a plus end directed microtubule motor, may antagonize the action of dynein because it is also located by BicD2 to the NPC. Therefore, at least in G2 phase, a large proportion of NPCs are tethered to microtubules via the dynein/dynactin complex, by the binding of BicD2 to Nup358.…”

Section: Association Of Interphase Nup358 With Microtubulesmentioning

confidence: 82%

“…One such adaptor is Bicaudal D (BICD). Using a biotinylation proximity assay and mass spectrometry peptide identification, as well as a yeast hybrid assay, Nup358 was identified as a candidate binding partner for BicD2 (Splinter et al, 2010). Coimmunoprecipitation with an anti-Nup358 antibody brought down BICD2BicD2, but not other dynein adaptors.…”

Section: Association Of Interphase Nup358 With Microtubulesmentioning

confidence: 99%

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Nuclear pore complex tethers to the cytoskeleton

Goldberg

2017

Seminars in Cell & Developmental Biology

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Section: Association Of Interphase Nup358 With Microtubulesmentioning

confidence: 82%

Section: Association Of Interphase Nup358 With Microtubulesmentioning

confidence: 99%

Nuclear pore complex tethers to the cytoskeleton

Goldberg

2017

Seminars in Cell & Developmental Biology

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“…No other high confidence G2 phase PLK1 interactors were identified. Several previously identified interactors were also identified that were mitosis-specific, including SPAG5/Astrin [25], ERCC-6L/PICH and NEDD1 [23,26,27], BICD2 [28], and BORA [23]. In addition, several novel PLK1-interacting proteins were identified; ATP5A1, ANKRD28/PP6-ARS-A, PPP6R2, TuFM/EF-Tu, HSPA9 and HNRNPF, although several of these have been previously identified as be PLK1 substrates (Table 1), but were found associated with the GFP-PBD in both G2 phase and mitotic samples.…”

Section: Jip4 Binds To Plk1 In G2 Phasementioning

confidence: 91%

JIP4 is a PLK1 binding protein that regulates p38MAPK activity in G2 phase

Pinder

Loo

Harrington

et al. 2015

Cellular Signalling

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Cell cycle progression from G2 phase into mitosis is regulated by a complex network of mechanisms, all of which finally control the timing of Cyclin B/CDK1 activation. PLK1 regulates a network of events that contribute to regulating G2/M phase progression. Here we have used a proteomics approach to identify proteins that specifically bind to the Polobox domain of PLK1. This identified a panel of proteins that were either associated with PLK1 in G2 phase and/or mitosis, the strongest interaction being with the MAPK scaffold protein JIP4. PLK1 binding to JIP4 was found in G2 phase and mitosis, and PLK1 binding was selfprimed by PLK1 phosphorylation of JIP4. PLK1 binding is required for JIP4-dependent p38MAPK activation in G2 phase during normal cell cycle progression, but not in either G2 phase or mitotic stress response. Finally, JIP4 is a target for caspase-dependent cleavage in mitotically arrested cells. The role for the PLK1-JIP4 regulated p38MAPK activation in G2 phase is unclear, but it does not affect either progression into or through mitosis.

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“…Interestingly, RANBP2 acts cooperatively with Nup153, the most nuclear of the NUPs, which contains a distinct zinc finger domain, in coordinating NE breakdown. RANBP2 also binds to BICD2 (homologous to Drosophila Bicaudal D), an adaptor between motor proteins and their cargo, and recruits BICD2 to NPCs in the G2 phase of the cell cycle (Splinter et al, 2010). BICD2 in turn regulates dynein-dynactin motor complexes at NPCs, and thus centrosome tethering to the NE prior to mitotic entry.…”

Section: Ranbp2 In Interphase Nucleocytoplasmic Transportmentioning

confidence: 99%