TBCCD1, a new centrosomal protein, is required for centrosome and Golgi apparatus positioning

Gonçalves, João; Nolasco, Sofia; Nascimento, Rute; Fanarraga, Mónica L.; Zabala, Juan Carlos; Soares, Helena

doi:10.1038/embor.2010.5

Cited by 53 publications

(69 citation statements)

References 25 publications

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“…This led to the hypothesis that TBCCD1 could share the GAP function of TBCC and RP2 and possibly have a microtubule-related role. However, this is contradicted by the inability of TBCCD1 to rescue the phenotypes of TBCC/CIN2 deletion in yeast (119). Indeed, TBCCD1 has an atypical TBCC domain in which the amino acid residues crucial for the GAP activity of TBCC and RP2 are not conserved (118,119).…”

Section: Centrosome-nucleus Connection Requires Tbccd1 a Tbcc-relatementioning

confidence: 75%

“…However, this is contradicted by the inability of TBCCD1 to rescue the phenotypes of TBCC/CIN2 deletion in yeast (119). Indeed, TBCCD1 has an atypical TBCC domain in which the amino acid residues crucial for the GAP activity of TBCC and RP2 are not conserved (118,119). In human cells, TBCCD1 localizes at the centrosome throughout the cell cycle, at the spindle midzone during anaphase, at the midbody during cytokinesis and at the basal bodies of primary and motile cilia (119).…”

Section: Centrosome-nucleus Connection Requires Tbccd1 a Tbcc-relatementioning

confidence: 91%

“…In C. reinhardtii, TBCCD1 localizes in the centrioles/basal bodies and in rhizoplasts, structures that connect them to each other and to the nucleus (118). TBCCD1 depletion by RNAi in human RPE-1 cells caused a marked increase in the nucleus-centrosome distance, with the centrosome often found at the cell periphery (119).…”

Section: Centrosome-nucleus Connection Requires Tbccd1 a Tbcc-relatementioning

confidence: 99%

“…Recently, a new TBCC-related protein, called TBCCD1 (TBCC domain-containing 1), was described both in the biflagellated green alga Chlamydomonas reinhardtii and human cells (118,119).…”

Section: Centrosome-nucleus Connection Requires Tbccd1 a Tbcc-relatementioning

confidence: 99%

“…Indeed, TBCCD1 has an atypical TBCC domain in which the amino acid residues crucial for the GAP activity of TBCC and RP2 are not conserved (118,119). In human cells, TBCCD1 localizes at the centrosome throughout the cell cycle, at the spindle midzone during anaphase, at the midbody during cytokinesis and at the basal bodies of primary and motile cilia (119). In C. reinhardtii, TBCCD1 localizes in the centrioles/basal bodies and in rhizoplasts, structures that connect them to each other and to the nucleus (118).…”

Section: Centrosome-nucleus Connection Requires Tbccd1 a Tbcc-relatementioning

confidence: 99%

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Revisiting the tubulin folding pathway: new roles in centrosomes and cilia

Gonçalves¹,

Tavares²,

Carvalhal³

et al. 2010

BioMolecular Concepts

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Centrosomes and cilia are critical eukaryotic organelles which have been in the spotlight in recent years given their implication in a myriad of cellular and developmental processes. Despite their recognized importance and intense study, there are still many open questions about their biogenesis and function. In the present article, we review the existing data concerning members of the tubulin folding pathway and related proteins, which have been identified at centrosomes and cilia and were shown to have unexpected roles in these structures.

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Section: Centrosome-nucleus Connection Requires Tbccd1 a Tbcc-relatementioning

confidence: 75%

Section: Centrosome-nucleus Connection Requires Tbccd1 a Tbcc-relatementioning

confidence: 91%

Section: Centrosome-nucleus Connection Requires Tbccd1 a Tbcc-relatementioning

confidence: 99%

“…Recently, a new TBCC-related protein, called TBCCD1 (TBCC domain-containing 1), was described both in the biflagellated green alga Chlamydomonas reinhardtii and human cells (118,119).…”

Section: Centrosome-nucleus Connection Requires Tbccd1 a Tbcc-relatementioning

confidence: 99%

Section: Centrosome-nucleus Connection Requires Tbccd1 a Tbcc-relatementioning

confidence: 99%

See 3 more Smart Citations

Revisiting the tubulin folding pathway: new roles in centrosomes and cilia

Gonçalves¹,

Tavares²,

Carvalhal³

et al. 2010

BioMolecular Concepts

Self Cite

View full text Add to dashboard Cite

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Tubulin Folding and Degradation

Serna

Zabala

2016

Encyclopedia of Life Sciences

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Synthesis of polypeptides inside a cell is an astonishing, complex and very efficient process. To reach the active state, proteins will have to face many different problems that in part are solved by molecular chaperones. Tubulins belong to one of the largest superfamilies of proteins with six conserved members. Different members have different roles although they share a general fold. Tubulins reach their final structure in an intricate pathway where different molecular chaperones are involved. Prefoldin and cytosolic chaperonin containing TCP1/TriC are required in the first part of the pathway, while tubulin folding cofactors (TBCs) are involved in the formation of the α‐ and β‐tubulin heterodimers. Later, their role in tubulin proteostasis as well as their implications in different neurodevelopmental disorders has been documented. Key Concepts Tubulins represent one of the largest families of genes and proteins. α‐ and β‐Tubulin heterodimers constitute the structural and functional subunit of microtubules (MTs). Folding of tubulins follows a sophisticated pathway involving several molecular chaperones. Formation of the αβ‐tubulin heterodimer is an extremely regulated process for it is involved in different lateral and longitudinal as well as microtubule associated proteins (MAPs) interactions. TBCs are molecular chaperones specifically required for αβ‐tubulin dimer formation. TBCs are shown to be involved in the release of tubulin monomers from the chaperonin during the folding pathway. The dissociation constant for the tubulin heterodimer has shown to be 10 −11 M and TBCs are required for an efficient tubulin dimer dissociation. TBCs are involved in tubulin proteostasis through dimer dissociation and tagging for proteasome recognition. The first 3D structure of a complex formed between α‐tubulin and two chaperones involved in the tubulin turnover cycle has been established. Genetic defects on TBCs are responsible of neurodevelopmental diseases.

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Orientation of Primary Cilia of Articular Chondrocytes in Three‐Dimensional Space

Farnum

Wilsman

2011

The Anatomical Record

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Primary cilia have functions as sensory organelles integral to signal transduction and establishment of cell polarity. In articular cartilage the primary cilium has been hypothesized to function as an antenna to sense the biomechanical environment, regulate the secretion of extracellular matrix components, and maintain cellular positional information, leading to high tissue anisotropy. We used analysis of electron microscopy serial sections to demonstrate positional attributes of the primary cilium of adult equine articular chondrocytes in situ. Data for $500 axonemes, comparing superficial to radiate chondrocytes from both load-bearing and non-load-bearing regions, were graphed using spherical co-ordinates y, u. The data demonstrate the axoneme has a definable orientation in 3D space differing in superficial and radiate zone chondrocytes, cells that differ by 90 in the orientation of their major axes to the articular surface. Axonemal orientation is more definable in load-bearing than in non-loadbearing areas. The position of emergence of the axoneme from the cell also is variable. In load-bearing regions of the superficial zone, extension of the axoneme is from the cellular side facing the subchondral bone. In radiate zone cells, axonemes extend from either face of the chondrocyte, that is, both toward the articular surface or toward the subchondral bone. In non-load-bearing regions this consistency is lost. These observations relate to current hypotheses concerning establishment of tissue anisotropy in articular cartilage during development, involving both migration of cells from the joint periphery and a restricted zone of division within the tissue resulting in the columnar arrangement of radiate zone cells. Anat Rec, 294:533-549, 2011. V V C 2011 Wiley-Liss, Inc.

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TBCCD1, a new centrosomal protein, is required for centrosome and Golgi apparatus positioning

Cited by 53 publications

References 25 publications

Revisiting the tubulin folding pathway: new roles in centrosomes and cilia

Revisiting the tubulin folding pathway: new roles in centrosomes and cilia

Tubulin Folding and Degradation

Orientation of Primary Cilia of Articular Chondrocytes in Three‐Dimensional Space

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