Mitotic Phosphorylation of the Dynein Light Intermediate Chain is Mediated by cdc2 Kinase

Dell, Karen R.; Turck, Christoph W.; Vale, Ronald D.

doi:10.1034/j.1600-0854.2000.010107.x

Cited by 55 publications

(45 citation statements)

References 36 publications

(24 reference statements)

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“…Glued and DIC were found to be hyperphosphorylated by cdk1 kinase at early mitotic phase [22]. Similarly, cdk1 also could phosphorylate b-tubulin and this modification appeared to impair both GTP binding to b-tubulin as well as formation of tubulin dimers [23].…”

Section: Discussionmentioning

confidence: 96%

Cell cycle-dependent mitochondrial biogenesis and dynamics in mammalian cells

Lee

Kim

Sun³

et al. 2007

Biochemical and Biophysical Research Communications

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Section: Discussionmentioning

confidence: 96%

Cell cycle-dependent mitochondrial biogenesis and dynamics in mammalian cells

Lee

Kim

Sun³

et al. 2007

Biochemical and Biophysical Research Communications

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“…LIC phosphorylation of the light intermediate chains appears to correlate with entry into mitosis (28) or regulation of membrane binding (29). However, functionally, cdc2 phosphorylation of LICs is linked to events at the metaphase/anaphase transition rather than early prometaphase (30).…”

Section: Discussionmentioning

confidence: 99%

Polo-like Kinase1 Is Required for Recruitment of Dynein to Kinetochores during Mitosis

Bader

Kasuboski

Winding

et al. 2011

Journal of Biological Chemistry

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Kinetochore dynein has been implicated in microtubule capture, correcting inappropriate microtubule attachments, chromosome movement, and checkpoint silencing. It remains unclear how dynein coordinates this diverse set of functions. Phosphorylation is responsible for some dynein heterogeneity (Whyte, J., Bader, J. R., Tauhata, S. B., Raycroft, M., Hornick, J., Pfister, K. K., Lane, W. S., Chan, G. K., Hinchcliffe, E. H., Vaughan, P. S., and Vaughan, K. T. (2008) J. Cell Biol. 183, 819 -834), and phosphorylated and dephosphorylated forms of dynein coexist at prometaphase kinetochores. In this study, we measured the impact of inhibiting polo-like kinase 1 (Plk1) on both dynein populations. Phosphorylated dynein was ablated at kinetochores after inhibiting Plk1 with a small molecule inhibitor (5-Cyano-7-nitro-2-(benzothiazolo-Noxide)-carboxamide) or chemical genetic approaches. The total complement of kinetochore dynein was also reduced but not eliminated, reflecting the presence of some dephosphorylated dynein after Plk1 inhibition. Although Plk1 inhibition had a profound effect on dynein, kinetochore populations of dynactin, spindly, and zw10 were not reduced. Plk1-independent dynein was reduced after p150Glued depletion, consistent with the binding of dephosphorylated dynein to dynactin. Plk1 phosphorylated dynein intermediate chains at Thr-89 in vitro and generated the phospho-Thr-89 phosphoepitope on recombinant dynein intermediate chains. Finally, inhibition of Plk1 induced defects in microtubule capture and persistent microtubule attachment, suggesting a role for phosphorylated dynein in these functions during prometaphase. These findings suggest that Plk1 is a dynein kinase required for recruitment of phosphorylated dynein to kinetochores.Cytoplasmic dynein plays important roles at spindle poles, the cell cortex, and kinetochores during mitosis. The mechanisms that allow dynein to associate specifically with each site remain unknown. One possibility is suggested by the identification of a novel mitotic phosphorylation site in the dynein intermediate chains (ICs) 2 (1). This phosphorylated form of dynein (phospho-Thr-89, pT89) is specific for kinetochores from nuclear envelope breakdown (NEB) to metaphase. Previous work suggests that pT89 dynein is recruited to kinetochores through a direct interaction with zw10 but undergoes dephosphorylation in response to bioriented microtubule attachment and chromosome alignment. This dephosphorylation of dynein shifts binding to dynactin and stimulates poleward transport of checkpoint proteins; a transition required for the silencing of the spindle assembly checkpoint at metaphase. Defects in this process induce metaphase arrest/delay.One prediction of this model is that dynein could interact with multiple proteins at kinetochores, depending on the degree of microtubule attachment, microtubule occupancy, and chromosome alignment. Consistent with this scenario, several mitotic proteins have been implicated in interacting with or anchoring kinetochore dynein, including dy...

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“…dynein and lead to inhibition of organelle movement (Addinall et al, 2001;Dell et al, 2000;Niclas et al, 1996;Sivaram et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

Rab11-FIP3 links the Rab11 GTPase and cytoplasmic dynein to mediate transport to the endosomal-recycling compartment

Horgan

Hanscom

Jolly

et al. 2010

Journal of Cell Science

178

176

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SummarySeveral protein families control intracellular transport processes in eukaryotic cells. Here, we show that the Rab11 GTPase effector protein Rab11-FIP3 (henceforth, FIP3) directly interacts with the dynein light intermediate chain 1 (DLIC-1, gene symbol DYNC1LI1) subunit of the cytoplasmic dynein 1 motor protein complex. We show that Rab11a, FIP3 and DLIC-1 form a ternary complex and that DLIC-1 colocalises with endogenous FIP3 and Rab11a in A431 cells. We demonstrate that association between FIP3 and DLIC-1 at the cell periphery precedes minus-end-directed microtubule-based transport, that FIP3 recruits DLIC-1 onto membranes, and that knockdown of DLIC-1 inhibits pericentrosomal accumulation of key endosomal-recycling compartment (ERC) proteins. In addition, we demonstrate that expression of a DLIC-1-binding truncation mutant of FIP3 disrupts the ability of ERC proteins to accumulate pericentrosomally. On the basis of these and other data, we propose that FIP3 links the Rab11 GTPase and cytoplasmic dynein to mediate transport of material from peripheral sorting endosomes to the centrally located ERC.

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Mitotic Phosphorylation of the Dynein Light Intermediate Chain is Mediated by cdc2 Kinase

Cited by 55 publications

References 36 publications

Cell cycle-dependent mitochondrial biogenesis and dynamics in mammalian cells

Cell cycle-dependent mitochondrial biogenesis and dynamics in mammalian cells

Polo-like Kinase1 Is Required for Recruitment of Dynein to Kinetochores during Mitosis

Rab11-FIP3 links the Rab11 GTPase and cytoplasmic dynein to mediate transport to the endosomal-recycling compartment

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