Entry - *608139 - CENTROMERE PROTEIN V; CENPV - OMIM
 
* 608139

CENTROMERE PROTEIN V; CENPV


Alternative titles; symbols

NUCLEAR PROTEIN p30


HGNC Approved Gene Symbol: CENPV

Cytogenetic location: 17p11.2   Genomic coordinates (GRCh38) : 17:16,342,537-16,353,469 (from NCBI)


TEXT

Cloning and Expression

Cronshaw et al. (2002) identified p30 as a constituent of a purified nucleoporin fraction from rat liver nuclei. Fluorescence-tagged p30 localized within nuclei of transfected HeLa cells, with enrichment at the nuclear periphery and around the nucleolus. It did not colocalize with the nuclear pore complex. Cronshaw et al. (2002) hypothesized that p30 may link peripheral nuclear structures with the nuclear interior.

Using the SH3-SH2 domain of human LYN (165120) as bait in a yeast 2-hybrid screen of a bone marrow expression library, Honda et al. (2009) cloned CENPV. The deduced 272-amino acid protein has an N-terminal polyproline stretch and a C-terminal cysteine-rich zinc finger domain. CENPV orthologs were detected in a range of species, including plants, but the proline-rich region was detected only in primates, rodents, birds, and amphibians, and long proline stretches were found only in primates. Northern blot analysis showed ubiquitous Cenpv expression in mouse tissues, with highest expression in testis, followed by small intestine, brain, and kidney. Immunofluorescence microscopy of mouse fibroblasts revealed colocalization of Cenpv with stabilized cytoplasmic microtubules. Western blot analysis of Ramos B cells detected CENPV at an apparent molecular mass of 40 kD.


Gene Function

Using a protein pull-down assay, Honda et al. (2009) confirmed the interaction between CENPV and the SH3-SH2 domain of LYN. In transfected HEK293 cells, CENPV expression resulted in the phosphorylation and activation of LYN and, to a lesser extent, FYN (137025). Mutation analysis showed that the polyproline domain of CENPV associated with the SH3 domains of LYN, FYN, and SRC (190090). Deletion of the zinc finger domain abrogated the interaction of CENPV with microtubules. Depletion of CENPV in a human breast cancer cell line via RNA interference impaired directional cell migration, but not cell growth or viability.


Mapping

Honda et al. (2009) stated that the CENPV gene maps to chromosome 17p11.2.


REFERENCES

  1. Cronshaw, J. M., Krutchinsky, A. N., Zhang, W., Chait, B. T., Matunis, M. J. Proteomic analysis of the mammalian nuclear pore complex. J. Cell Biol. 158: 915-927, 2002. [PubMed: 12196509, images, related citations] [Full Text]

  2. Honda, Z., Suzuki, T., Honda, H. Identification of CENP-V as a novel microtubule-associating molecule that activates Src family kinases through SH3 domain interaction. Genes Cells 14: 1383-1394, 2009. [PubMed: 19930468, related citations] [Full Text]


Contributors:
Patricia A. Hartz - updated : 12/14/2010
Creation Date:
Patricia A. Hartz : 9/30/2003
mgross : 01/05/2011
terry : 12/14/2010
mgross : 9/30/2003

* 608139

CENTROMERE PROTEIN V; CENPV


Alternative titles; symbols

NUCLEAR PROTEIN p30


HGNC Approved Gene Symbol: CENPV

Cytogenetic location: 17p11.2   Genomic coordinates (GRCh38) : 17:16,342,537-16,353,469 (from NCBI)


TEXT

Cloning and Expression

Cronshaw et al. (2002) identified p30 as a constituent of a purified nucleoporin fraction from rat liver nuclei. Fluorescence-tagged p30 localized within nuclei of transfected HeLa cells, with enrichment at the nuclear periphery and around the nucleolus. It did not colocalize with the nuclear pore complex. Cronshaw et al. (2002) hypothesized that p30 may link peripheral nuclear structures with the nuclear interior.

Using the SH3-SH2 domain of human LYN (165120) as bait in a yeast 2-hybrid screen of a bone marrow expression library, Honda et al. (2009) cloned CENPV. The deduced 272-amino acid protein has an N-terminal polyproline stretch and a C-terminal cysteine-rich zinc finger domain. CENPV orthologs were detected in a range of species, including plants, but the proline-rich region was detected only in primates, rodents, birds, and amphibians, and long proline stretches were found only in primates. Northern blot analysis showed ubiquitous Cenpv expression in mouse tissues, with highest expression in testis, followed by small intestine, brain, and kidney. Immunofluorescence microscopy of mouse fibroblasts revealed colocalization of Cenpv with stabilized cytoplasmic microtubules. Western blot analysis of Ramos B cells detected CENPV at an apparent molecular mass of 40 kD.


Gene Function

Using a protein pull-down assay, Honda et al. (2009) confirmed the interaction between CENPV and the SH3-SH2 domain of LYN. In transfected HEK293 cells, CENPV expression resulted in the phosphorylation and activation of LYN and, to a lesser extent, FYN (137025). Mutation analysis showed that the polyproline domain of CENPV associated with the SH3 domains of LYN, FYN, and SRC (190090). Deletion of the zinc finger domain abrogated the interaction of CENPV with microtubules. Depletion of CENPV in a human breast cancer cell line via RNA interference impaired directional cell migration, but not cell growth or viability.


Mapping

Honda et al. (2009) stated that the CENPV gene maps to chromosome 17p11.2.


REFERENCES

  1. Cronshaw, J. M., Krutchinsky, A. N., Zhang, W., Chait, B. T., Matunis, M. J. Proteomic analysis of the mammalian nuclear pore complex. J. Cell Biol. 158: 915-927, 2002. [PubMed: 12196509] [Full Text: https://doi.org/10.1083/jcb.200206106]

  2. Honda, Z., Suzuki, T., Honda, H. Identification of CENP-V as a novel microtubule-associating molecule that activates Src family kinases through SH3 domain interaction. Genes Cells 14: 1383-1394, 2009. [PubMed: 19930468] [Full Text: https://doi.org/10.1111/j.1365-2443.2009.01355.x]


Contributors:
Patricia A. Hartz - updated : 12/14/2010

Creation Date:
Patricia A. Hartz : 9/30/2003

Edit History:
mgross : 01/05/2011
terry : 12/14/2010
mgross : 9/30/2003