Tubulin-binding cofactor C domain-containing protein TBCCD1 orchestrates cytoskeletal filament formation

André, Jane; Harrison, S.C.; Towers, Katie; Qi, Xin; Vaughan, Sue; McKean, Paul G.; Ginger, Michael L.

doi:10.1242/jcs.136515

Cited by 29 publications

(36 citation statements)

References 37 publications

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“…Moreover, dis initial cells were markedly larger than the wild-type equivalents and their Golgi network was more abundant and fragmented (shorter cisternae). Increased cell size and disorganization of the Golgi apparatus have been observed in TBCCd1-depleted human and trypanosome cells (Gonçalves et al, 2010;André et al, 2013). The role of TBCCd1 in regulating organelle positioning and microtubule and Golgi architecture, highlighted by our study, can therefore be traced back to the crown divergence of the major eukaryotic groups, more than a billion years ago (Eme et al, 2014).…”

Section: Dis Encodes a Tbcc Domain Protein With A Conserved Role In Imentioning

confidence: 57%

“…RP2 is also thought to be involved in microtubule assembly but the role TBCCd1 is less clear. Phenotypic analyses have shown that TBCCd1 plays an important role in positioning organelles within the cell in diverse organisms (Feldman and Marshall, 2009;André et al, 2013), but the molecular mechanism through which this protein acts is unclear and may not involve direct effects on microtubule dynamics (Gonçalves et al, 2010). These previous studies prompted us to compare intracellular features of germinating dis initial cells with those of the wild type.…”

Section: Dis Encodes the Conserved Protein Tbccd1mentioning

confidence: 99%

“…TBCCd1 has been localized to the centrosome and the Golgi in organisms as diverse as humans, Chlamydomonas, and trypanosomes, and loss-of-function experiments have indicated a conserved and important role for TBCCd1 in various aspects of the organization of cellular architecture in these diverse eukaryote groups (André et al, 2013;Feldman and Marshall, 2009;Gonçalves et al, 2010). Loss or knockdown of TBCCd1 has severe consequences for cell morphology, for example, leading to alterations in the shape and motility of human cells (Gonçalves et al, 2010), mitotic defects in trypanosomes (André et al, 2013), and defects both in flagella number and functioning and during cell division due to misorientation of the mitotic spindle in Chlamydomonas (Feldman and Marshall, 2009).…”

Section: Dis Encodes a Tbcc Domain Protein With A Conserved Role In Imentioning

confidence: 99%

“…Loss or knockdown of TBCCd1 has severe consequences for cell morphology, for example, leading to alterations in the shape and motility of human cells (Gonçalves et al, 2010), mitotic defects in trypanosomes (André et al, 2013), and defects both in flagella number and functioning and during cell division due to misorientation of the mitotic spindle in Chlamydomonas (Feldman and Marshall, 2009). Although we did not detect any defects in flagella structure or centriole positioning in Ectocarpus dis mutants, the initial cells of these mutants did show defects in the positioning of the nucleus and an atypical microtubule network during germination.…”

Section: Dis Encodes a Tbcc Domain Protein With A Conserved Role In Imentioning

confidence: 99%

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DISTAG/TBCCd1 Is Required for Basal Cell Fate Determination in Ectocarpus

et al. 2017

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Brown algae are one of the most developmentally complex groups within the eukaryotes. As in many land plants and animals, their main body axis is established early in development, when the initial cell gives rise to two daughter cells that have apical and basal identities, equivalent to shoot and root identities in land plants, respectively. We show here that mutations in the Ectocarpus DISTAG (DIS) gene lead to loss of basal structures during both the gametophyte and the sporophyte generations. Several abnormalities were observed in the germinating initial cell in dis mutants, including increased cell size, disorganization of the Golgi apparatus, disruption of the microtubule network, and aberrant positioning of the nucleus. DIS encodes a TBCCd1 protein, which has a role in internal cell organization in animals, Chlamydomonas reinhardtii, and trypanosomes. Our study highlights the key role of subcellular events within the germinating initial cell in the determination of apical/basal cell identities in a brown alga and emphasizes the remarkable functional conservation of TBCCd1 in regulating internal cell organization across extremely distant eukaryotic groups.

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Section: Dis Encodes a Tbcc Domain Protein With A Conserved Role In Imentioning

confidence: 57%

Section: Dis Encodes the Conserved Protein Tbccd1mentioning

confidence: 99%

Section: Dis Encodes a Tbcc Domain Protein With A Conserved Role In Imentioning

confidence: 99%

Section: Dis Encodes a Tbcc Domain Protein With A Conserved Role In Imentioning

confidence: 99%

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DISTAG/TBCCd1 Is Required for Basal Cell Fate Determination in Ectocarpus

et al. 2017

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“…The TbMORN1 (40 kDa) molecules in the complex are arranged in a linear macromolecular filament of ϳ0.2 by 2 m whose posterior end is tightly coiled around the FPN, producing an overall fishhook-shaped morphology (13). At least nine other proteins are known to partially or wholly associate with this complex: TbLRRP1, TBCCD1, and seven currently uncharacterized proteins identified in a screen using proximity-dependent biotinylation (14)(15)(16). Both the TbMORN1 filament and the FPC are strongly associated with the microtubule-based cytoskeleton.…”

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confidence: 99%

A MORN Repeat Protein Facilitates Protein Entry into the Flagellar Pocket of Trypanosoma brucei

Morriswood

Schmidt

2015

Eukaryot Cell

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The parasite Trypanosoma brucei lives in the bloodstream of infected mammalian hosts, fully exposed to the adaptive immune system. It relies on a very high rate of endocytosis to clear bound antibodies from its cell surface. All endo-and exocytosis occurs at a single site on its plasma membrane, an intracellular invagination termed the flagellar pocket. Coiled around the neck of the flagellar pocket is a multiprotein complex containing the repeat motif protein T. brucei MORN1 (TbMORN1). In this study, the phenotypic effects of TbMORN1 depletion in the mammalian-infective form of T. brucei were analyzed. Depletion of TbMORN1 resulted in a rapid enlargement of the flagellar pocket. Dextran, a polysaccharide marker for fluid phase endocytosis, accumulated inside the enlarged flagellar pocket. Unexpectedly, however, the proteins concanavalin A and bovine serum albumin did not do so, and concanavalin A was instead found to concentrate outside it. This suggests that TbMORN1 may have a role in facilitating the entry of proteins into the flagellar pocket.T rypanosoma brucei is an important parasite of humans and domestic animals in sub-Saharan Africa, as the causative agent of sleeping sickness and nagana, respectively. Its complex life cycle involves transitions between tsetse fly vectors (its definitive hosts) and mammalian intermediate hosts. This life cycle involves a number of different cell stages, of which the procyclic form (found in the tsetse fly) and the slender bloodstream form (BSF) (found in the mammalian bloodstream) are the best studied in a laboratory setting. The procyclic form and the BSF of T. brucei share similar cytoskeletal architectures (1, 2).The principal feature of this cytoskeleton is a corset of microtubules that lie directly underneath the plasma membrane and impart to the cell its distinctive shape (3). A single invagination of the plasma membrane, termed the flagellar pocket (FP), constitutes a distinct subdomain and is found at the posterior end of the cell (4). The FP is the site of all endo-and exocytic traffic (5, 6). Abutting the FP membrane is a basal body that nucleates the single flagellum of the trypanosome cell. The flagellum exits the FP and is adhered longitudinally to the cell body along a left-handed helical path (7). Once outside the FP, the axoneme of the flagellum is paralleled by an associated intraflagellar structure called the paraflagellar rod (PFR). The PFR is composed of a paracrystalline lattice and is associated with cellular motility (8). Nucleated adjacent to the basal body is a specialized microtubule quartet that traces around the FP and then underlies the flagellum as far as the anterior end of the cell (4).The small cylinder of membrane that connects the FP to the rest of the plasma membrane constitutes a third subdomain and is called the flagellar pocket neck (FPN) (4). A number of discrete cytoskeletal structures cluster around the FPN membrane on its cytoplasmic face. Of these, the best characterized is an electrondense horseshoe-shaped structure named th...

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Tbccd1

Gonçalves¹,

Soares²

2016

Encyclopedia of Signaling Molecules

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Tubulin-binding cofactor C domain-containing protein TBCCD1 orchestrates cytoskeletal filament formation

Cited by 29 publications

References 37 publications

DISTAG/TBCCd1 Is Required for Basal Cell Fate Determination in Ectocarpus

DISTAG/TBCCd1 Is Required for Basal Cell Fate Determination in Ectocarpus

A MORN Repeat Protein Facilitates Protein Entry into the Flagellar Pocket of Trypanosoma brucei

Tbccd1

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