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Centrin4p, a novel mammalian centrin specifically expressed in ciliated cells.

ABSTRACT: Centriole assembly plays an important role in centrosome duplication during the cell cycle and is a prerequisite for cilia formation during the differentiation of ciliated cells. In spite of numerous investigations, the molecular machinery that governs centriole/basal body formation remains enigmatic. Recent reports suggest that the ubiquitously expressed mammalian centrins, centrin2p and centrin3p, could be involved in the centriole duplication process. To better understand the specific functions of these proteins, we performed a systematic search for novel mammalian centrins. We isolated a cDNA and the corresponding gene coding for a novel murine centrin, centrin4p, which is more closely related to centrin2p. Like centrin2p, centrin4p accumulates to centrioles and procentrioles when ectopically expressed in HeLa cells. However, centrin4p possesses two splice variants that do not localize to centrioles, suggesting a posttranscriptional regulation mechanism. We also observed that centrin4p does not share the same centriolar targeting properties with centrin2p and 3p, indicating that these proteins could recognize different centriolar partners. Centrin4 mRNA possesses a restricted expression profile and is only detected in brain, kidney, lung, and ovary. In brain, centrin4p is exclusively expressed in ependymal and choroidal ciliated cells where it is localized to basal bodies. Together, our present data suggest that centrin4p could be more specifically involved in basal bodies assembly or in a subsequent step of ciliogenesis.

SUBMITTER: Gavet O

PROVIDER: S-EPMC165080 | biostudies-literature | 2003 May

REPOSITORIES: biostudies-literature

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Centrin4p, a novel mammalian centrin specifically expressed in ciliated cells.

Gavet Olivier O Alvarez Chantale C Gaspar Patricia P Bornens Michel M

Molecular biology of the cell 20030206 5

Centriole assembly plays an important role in centrosome duplication during the cell cycle and is a prerequisite for cilia formation during the differentiation of ciliated cells. In spite of numerous investigations, the molecular machinery that governs centriole/basal body formation remains enigmatic. Recent reports suggest that the ubiquitously expressed mammalian centrins, centrin2p and centrin3p, could be involved in the centriole duplication process. To better understand the specific functio ...[more]

PMID: 12802058

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Project description:Syntaxin 1A has been identified previously as a neural-cell-specific, membrane-anchored receptor protein required for docking and fusion of synaptic vesicles with the presynaptic plasma membrane. Syntaxin 1A consists of 288 amino acid residues including a 265-residue N-terminal region exposed to the cytoplasm and a C-terminal hydrophobic stretch of 23 residues believed to anchor syntaxin to the plasma membrane. Using a human fat-cell library we have isolated a novel cDNA clone of syntaxin 1A containing an insert of 91 bp in codon 226. This insert and subsequent frame shift generated a cDNA that codes for a truncated protein of 260 residues without the C-terminal transmembrane domain characteristic of the syntaxin family. Analysis of the deduced amino acid sequence of the new cDNA clone, termed syntaxin 1C, showed that it was identical for the first 226 residues with the previously described neural syntaxin 1A, and diverged thereafter. The truncated protein lacked the botulinum neurotoxin C cleavage site (Lys253-Ala254), a feature of the syntaxin 1A protein, because of the novel C-terminal domain of 34 residues. The new C-terminal region contained a single cysteine residue and was moderately rich in proline, with three repeats of a PXP motif. The insert occurred within the region encoding the coiled-coil motifs required for interactions with synaptobrevin, alpha-SNAP (SNAP being soluble N-ethylmaleimide-sensitive factor attachment protein) and n-Sec1/Munc-18 (n-Sec1 being the rat brain homologue of yeast Sec1p and Munc-18 the mammalian homologue of Caenorhabditis elegans unc-18, but five residues outside the domain previously mapped as being required for binding SNAP-25. Interaction studies in vitro suggested that unlike syntaxin 1A, which binds to both Munc-18a and- 18b, syntaxin 1C binds only to Munc-18b. The new isoform syntaxin 1C, which might be generated by alternative splicing of the syntaxin 1 gene, was expressed in several human tissues, including brain. Immuno-precipitation and immunoblotting with the monoclonal antibody HPC-1 and a polyclonal antibody raised against a peptide corresponding to the unique C-terminal 35 residues of syntaxin 1C failed to detect syntaxin 1C at the protein level in extracts of muscle, fat or brain.

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Centrin4p, a novel mammalian centrin specifically expressed in ciliated cells.

Publications

Centrin4p, a novel mammalian centrin specifically expressed in ciliated cells.

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