Difference between revisions of "Phosphatase Subfamily PTPDC1"

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(Evolution)
 
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===Domain Structure===
 
===Domain Structure===
PTPDC1 typically has an N-terminal phosphatase domain and usually an extended, poorly-conserved C-terminal region. The Monosiga homolog has an N-terminal PH domain extension.
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PTPDC1 typically has an N-terminal phosphatase domain and usually an extended C-terminal region that includes a novel conserved domain most similar to the RhoGAP family (unpublished). The Monosiga homolog has an N-terminal PH domain extension.
  
 
===Functions===
 
===Functions===

Latest revision as of 18:30, 22 March 2017

Phosphatase Classification: Superfamily CC1: Family DSP: Subfamily PTPDC1

Evolution

PTPDC1 is found in holozoans but lost from Drosophila and most other insects. Distant homologs are also seen in a number of protist genomes. The pattern is near-identical to other cilia-associated proteins (the ciliome) that are lost in species that lack cilia.

Domain Structure

PTPDC1 typically has an N-terminal phosphatase domain and usually an extended C-terminal region that includes a novel conserved domain most similar to the RhoGAP family (unpublished). The Monosiga homolog has an N-terminal PH domain extension.

Functions

Mouse PTPDC1 has been proposed as a cilia gene by tissue-specific expression [1] and RNAi knockdown [2] and implicated in centriole duplication and cytokinesis [3]

References

  1. McClintock TS, Glasser CE, Bose SC, and Bergman DA. Tissue expression patterns identify mouse cilia genes. Physiol Genomics. 2008 Jan 17;32(2):198-206. DOI:10.1152/physiolgenomics.00128.2007 | PubMed ID:17971504 | HubMed [McClintock]
  2. Lai CK, Gupta N, Wen X, Rangell L, Chih B, Peterson AS, Bazan JF, Li L, and Scales SJ. Functional characterization of putative cilia genes by high-content analysis. Mol Biol Cell. 2011 Apr;22(7):1104-19. DOI:10.1091/mbc.E10-07-0596 | PubMed ID:21289087 | HubMed [Lai]
  3. Zineldeen DH, Shimada M, Niida H, Katsuno Y, and Nakanishi M. Ptpcd-1 is a novel cell cycle related phosphatase that regulates centriole duplication and cytokinesis. Biochem Biophys Res Commun. 2009 Mar 13;380(3):460-6. DOI:10.1016/j.bbrc.2009.01.113 | PubMed ID:19284988 | HubMed [Zineldeen]
All Medline abstracts: PubMed | HubMed