Coordination of adjacent domains mediates TACC3–ch-TOG–clathrin assembly and mitotic spindle binding

Hood, Fiona E.; Williams, Samantha; Burgess, Selena G.; Richards, Mark W.; Röth, Daniel; Straube, Anne; Pfuhl, Mark; Bayliss, Richard; Royle, Stephen

doi:10.1083/jcb.201211127

Cited by 78 publications

(193 citation statements)

References 51 publications

(129 reference statements)

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“…9E). The association of the TACC domain with the microtubule lattice, as well as its involvement in microtubule growth, was consistent with previous findings by other groups (30,36).…”

Section: Discussionsupporting

confidence: 82%

“…This process is believed to involve the recruitment of the microtubule-associated protein X-Map215 to the K-fibers (36). Our finding that the TACC domain exhibits intrinsic microtubule nucleating activity (Fig.…”

Section: Discussionmentioning

confidence: 53%

“…We next examined the role of the TACC domain of TACC3 in this rescue effect. We used a GFP-tagged C-terminal construct consisting of amino acid residues 500 -838 of TACC3 (GFP-TACC3(500 -838), which largely consists of the TACC(638 -838) domain and has been shown to localize much more efficiently to the spindle poles compared with the TACC-only domain (36). We transfected HeLa cells with TACC3-3Ј-UTR-siRNA along with the GFP-TACC3(500 -838) that lacked the 3Ј-UTR.…”

Section: Tacc3 Is Required For Astral Microtubule Assembly Andmentioning

confidence: 99%

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TACC3 Protein Regulates Microtubule Nucleation by Affecting γ-Tubulin Ring Complexes

Singh

Thomas

Gireesh

et al. 2014

Journal of Biological Chemistry

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Background:The nucleation of centrosomal microtubules requires proper regulation of the ␥-tubulin complex proteins. Results: TACC3 depletion impairs microtubule nucleation and disrupts the assembly of the ␥-tubulin ring complex components and their localization at the centrosome. Conclusion: TACC3 is involved in microtubule nucleation and in stabilization of the ␥-tubulin ring complex. Significance: These results provide additional insights into the regulation of centrosomal microtubule nucleation.

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“…9E). The association of the TACC domain with the microtubule lattice, as well as its involvement in microtubule growth, was consistent with previous findings by other groups (30,36).…”

Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 53%

Section: Tacc3 Is Required For Astral Microtubule Assembly Andmentioning

confidence: 99%

See 1 more Smart Citation

TACC3 Protein Regulates Microtubule Nucleation by Affecting γ-Tubulin Ring Complexes

Singh

Thomas

Gireesh

et al. 2014

Journal of Biological Chemistry

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“…In the M phase, microtubule-stabilizing protein TACC3 is phosphorylated by Aurora kinase A (25,26). Activated TACC3 associates with the ankle of clathrin and combines with chTOG to form the CHC17-TACC3-chTOG complex (27). Clathrin must play an important role in the CHC17-TACC3-chTOG complex because K-fibers develop defects when CLC is cross-linked in S phase to inactivate CHC17 (26).…”

Section: Centrosome and Mitotic Spindle Integritymentioning

confidence: 99%

Novel clathrin activity: developments in health and disease

Ybe

2014

Biomolecular Concepts

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Clathrin self-assembles into a coat around vesicles filled with cargo such as nutrients, hormones, and proteins destined for degradation. Recent developments indicate clathrin is not a specialist, but is involved in different processes relevant to health and disease. Clathrin is used to strengthen centrosomes and mitotic spindles essential for chromosome segregation in cell division. In Wnt signaling, clathrin is a component of signalosomes on the plasma membrane needed to produce functional Wnt receptors. In glucose metabolism, a muscle-specific isoform, CHC22 clathrin, is key to the formation of storage compartments for GLUT4 receptor, and CHC22 dysfunction has been tied to type 2 diabetes. The activity of clathrin to self-assemble and to work with huntingtin-interacting proteins to organize actin is exploited by Listeria and enteropathic Escherichia coli in their infection pathways. Finally, there is an important connection between clathrin and human malignancies. Clathrin is argued to help transactivate tumor suppressor p53 that controls specific genes in DNA repair and apoptosis. However, this is debatable because trimeric clathrin must be made monomeric. To get insight on how the clathrin structure could be converted, the crystal structure of the trimerization domain is used in the development of the detrimerization switch hypothesis. This novel hypothesis will be relevant if connections continue to be found between CHC17 and p53 anti-cancer activity in the nucleus.

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“…13 For example, in mitotic cells, clathrin forms a protein complex with two spindle pole proteins, transforming acidic coiled-coil protein 3 (TACC3) and colonic hepatic tumor overexpressed gene (ch-TOG). These proteins help stabilize the mitotic spindle microtubules, [14][15][16][17][18] an event requiring an interaction with clathrin and clathrin localization to the spindle. 13,15,18 Beyond regulating cell surface area, the reason for continued endocytosis and decreased membrane recycling during mitosis remains elusive.…”

mentioning

confidence: 99%

A new role for Rab GTPases during early mitotic stages

2014

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A recent study revealed new roles for the Rab11 GTPase during mitosis. Rab11 is involved in recycling endosome localization to mitotic spindle poles via dynein-mediated transport. This process is in contrast to Golgi membranes, which disperse in mitosis and do not appear to directly contribute to mitotic functions. Rab11-depletion prevents recycling endosome organization at spindle poles, delays mitotic progression, and disrupts spindle pole protein recruitment, astral microtubule organization, and mitotic spindle orientation. However, Rab11 is not the only endocytic and/or trafficking protein that regulates mitotic progression. Clathrin and two small GTPases (Rab6A', Rab5) play key roles in spindle organization and function. In this commentary, we discuss the roles of all these canonical endocytic and membrane trafficking proteins during mitosis and speculate on possible crosscommunication between them and their molecular pathways that ensure faithful progression through mitosis. IntroductionIt has been known for some time that the recycling endosome is organized around the "centrosome region" 1 . However, a direct relationship between these intracellular elements remained unclear until 2012 when electron microscopy revealed an intimate interaction with a substructure of the centrosome, the mother centriole appendages.2 Mother centriole appendages have become a focus of interest because they functionally define the "older" centriole of the centriole pair. This has important consequences in biology. For example, the older centriole remains in the stem cell, where Rab11-membranes accumulate, while the cell with the younger centrosome undergoes differentiation. 3,4 The mother centriole also templates cilia formation 5 and regulates membrane recycling through Rab11. 2The role of the mother centriole was further identified to modulate Rab11-activity through organization of recycling endosome machinery.2 If appendages were disrupted, recycling endosome machinery (e.g., the exocyst and the Rab11 GTPase Activating Protein, EVI5) were dispersed.2 However, what this study did not demonstrate was whether recycling endosomes contributed to the organization and function of the centrosome. A follow-up study went on to show that the recycling endosome contributes to the organization of the mitotic spindle poles and organization of the spindle. A Novel Role for Rab11-Endosomes in Spindle Pole MaturationEarlier work in Caenorhabditis elegans identified a role for Rab11-endosomes during mitosis. 6,7 These studies showed that depletion of Rab11 caused spindle misalignment through disruption of astral microtubule arrays.

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Coordination of adjacent domains mediates TACC3–ch-TOG–clathrin assembly and mitotic spindle binding

Abstract: Aurora A phosphorylation-induced interaction of TACC3 and clathrin coordinates adjacent domains in each protein to create a microtubule-binding interface, whereas a distinct site in TACC3 recruits ch-TOG to mitotic spindles.

Cited by 78 publications

References 51 publications

TACC3 Protein Regulates Microtubule Nucleation by Affecting γ-Tubulin Ring Complexes

TACC3 Protein Regulates Microtubule Nucleation by Affecting γ-Tubulin Ring Complexes

Novel clathrin activity: developments in health and disease

A new role for Rab GTPases during early mitotic stages

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