The calcium-binding protein cell division cycle 31 of Saccharomyces cerevisiae is a component of the half bridge of the spindle pole body.

Spang, Anne; Courtney, Iain; Fackler, Ursel; Matzner, Monika; Schiebel, Elmar

doi:10.1083/jcb.123.2.405

Cited by 164 publications

(194 citation statements)

References 44 publications

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“…The simplest situation is found in yeast; the cdc31 gene product, a most divergent centrin, is localized to the spindle pole body and required for spindle pole body duplication (Baum et al, 1986). Both molecular and genetic evidence indicates that cdc31 is a unique, and an essential, gene (Spang et al, 1993). In humans, although centrin appears to be restricted to a centrosomal localization, two centrin genes have been characterized (Lee and Huang, 1993;Errabolu et al, 1994).…”

Section: Discussionmentioning

confidence: 99%

Characterization of Centrin Genes in Paramecium

Madeddu

Klotz

Caër³

et al. 1996

European Journal of Biochemistry

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Centrins are highly conserved, ubiquitous cytoskeletal components which belong to the EF-hand superfamily of Caz+-modulated proteins. We report here the molecular characterization of new members of the centrin family, Paranzecium centrins. Previous studies described the organization of the infraciliary lattice (ICL), the innermost cortical cytoskeletal network of Paramecium, and showed that it was composed of a set of low-molecular-mass, Ca*+-binding polypeptides [Garreau de Loubresse, N., Klotz, C., Vigues, B., Rutin, J. & Beisson, J. ) Bid. Cell 71, 217-2251. In this paper we show that these polypeptides are recognized by specific anti-centrin polyclonal antibodies. Their microsequences revealed four distinct N-termini. For one of them, ICLI, N-terminal and internal peptide sequences were used for PCR amplification and cloning of a DNA fragment containing a complete centrin coding sequence. The deduced amino acid sequence presents about 50% identity with those of centrins from other species. Further molecular analysis allowed us to identify two additional closely related, co-expressed ICLl genes, providing the first example of a centrin multigenic family in a microorganism.

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Section: Discussionmentioning

confidence: 99%

Characterization of Centrin Genes in Paramecium

Madeddu

Klotz

Caër³

et al. 1996

European Journal of Biochemistry

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“…The representation of Spc29 in between Spc110 and Spc42 is highly schematic, as the exact nature of its function as part of the Spc110 complex remains to be established. Cdc31, Kar1, Mps3, and Sfi1 (Baum et al 1986;Rose and Fink 1987;Spang et al 1993Spang et al , 1995Biggins and Rose 1994;Jaspersen et al 2002;Kilmartin 2003;Li et al 2006). Kar1 and the SUN domain protein Mps3 each contain a single membrane-spanning domain (Rose and Fink 1987;Jaspersen et al 2002).…”

Section: Structure and Duplication Cycle Of Yeast Spbsmentioning

confidence: 99%

The Centrosome and Its Duplication Cycle

Hagan

Glover

2015

Cold Spring Harb Perspect Biol

210

194

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“…The SPB is a proteinaceous structure that is embedded in the nuclear envelope, and its duplication marks exit from the G 1 phase and the onset of chromosome duplication. The composition of the SPB has been defined, and the steps that lead to its duplication have been studied extensively using biochemical, genetic, and microscopic methods (3,5,6,18,24,28,30,43,44). An important component of the SPB is Cdc31 (3, 13), which in yeast is encoded by the essential CDC31 gene.…”

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confidence: 99%

Centrin/Cdc31 Is a Novel Regulator of Protein Degradation

Chen

Madura

2008

Molecular and Cellular Biology

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Rad23 is required for efficient protein degradation and performs an important role in nucleotide excision repair. Saccharomyces cerevisiae Rad23, and its human counterpart (hHR23), are present in a complex containing the DNA repair factor Rad4 (termed XPC, for xeroderma pigmentosum group C, in humans). XPC/ hHR23 was also reported to bind centrin-2, a member of the superfamily of calcium-binding EF-hand proteins. We report here that yeast centrin, which is encoded by CDC31, is similarly present in a complex with Rad4/Rad23 (called NEF2). The interaction between Cdc31 and Rad23/Rad4 varied by growth phase and reflected oscillations in Cdc31 levels. Strikingly, a cdc31 mutant that formed a weaker interaction with Rad4 showed sensitivity to UV light. Based on the dual function of Rad23, in both DNA repair and protein degradation, we questioned if Cdc31 also participated in protein degradation. We report here that Cdc31 binds the proteasome and multiubiquitinated proteins through its carboxy-terminal EF-hand motifs. Moreover, cdc31 mutants were highly sensitive to drugs that cause protein damage, failed to efficiently degrade proteolytic substrates, and formed altered interactions with the proteasome. These findings reveal for the first time a new role for centrin/Cdc31 in protein degradation.The microtubule organizing center regulates cytoskeletal integrity, and is termed the centrosome in higher eukaryotes, and the spindle pole-body (SPB) in yeast. The duplication of the SPB/centrosome is a key event that initiates entry into the cell cycle. The SPB is a proteinaceous structure that is embedded in the nuclear envelope, and its duplication marks exit from the G 1 phase and the onset of chromosome duplication. The composition of the SPB has been defined, and the steps that lead to its duplication have been studied extensively using biochemical, genetic, and microscopic methods (3,5,6,18,24,28,30,43,44). An important component of the SPB is Cdc31 (3, 13), which in yeast is encoded by the essential CDC31 gene. CDC31 was isolated as a suppressor of kar1, a mutant that is unable to duplicate the SPB at the nonpermissive temperature (6). As with kar1, defects in CDC31 (cdc31) also cause G 1 phase arrest, due to a failure in SPB duplication (48). Intriguingly, the kar1 defect was suppressed by Dsk2 (5), which has functional and structural resemblance to Rad23 (15,29,34,40).The three centrin proteins that are expressed in human cells (30, 31) display differential tissue-specific levels (27,36,49). However, all three isoforms share the key structural features that are present in EF-hand proteins (32). Human CEN3 is closely related to Cdc31 and can interfere with SPB duplication when overexpressed in yeast (30). An N-terminal regulatory domain is proposed to regulate the activity of the C-terminal domain, possibly through Ca 2ϩ -mediated signaling (42). The C terminus binds various cellular proteins (1, 7, 11, 12, 16, 19-23, 28, 37, 46, 50), although the effect of these interactions in regulating growth control is not well ...

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The calcium-binding protein cell division cycle 31 of Saccharomyces cerevisiae is a component of the half bridge of the spindle pole body.

Cited by 164 publications

References 44 publications

Characterization of Centrin Genes in Paramecium

Characterization of Centrin Genes in Paramecium

The Centrosome and Its Duplication Cycle

Centrin/Cdc31 Is a Novel Regulator of Protein Degradation

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