Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2007-2-19
pubmed:abstractText
PP5 is a member of the PPP family of serine/threonine protein phosphatases and is present in all eukaryotes. We previously cloned and characterized a PP5 homologue from Trypanosoma brucei. Here, we synchronized the T. brucei procyclic form by hydroxyurea treatment and showed that TbPP5 expression is regulated during cell cycle progression. TbPP5 transcript and protein levels were maximal in the G1 phase of the cell cycle, and reduced about 3-fold in the G2/M phase. To further evaluate its function, TbPP5 expression was depleted in both procyclic and bloodstream forms of T. brucei by RNA interference. In the procyclic form, TbPP5 knockdown resulted in a moderate reduction in cell growth. However, in the bloodstream form, ablation of TbPP5 caused an 8-fold decrease in cell growth. Furthermore, TbPP5 overexpression conferred the ability of procyclic cells to grow in serum-deprived conditions suggesting that TbPP5 acts downstream of serum factor-induced growth in T. brucei. Taken together; these findings suggest that a serum factor (or factors) induces up-regulation of TbPP5 expression during the G1 phase, which is required for proper cell growth.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-3395
pubmed:author
pubmed:issnType
Print
pubmed:volume
92
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1152-61
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Functional characterization of the serine/threonine protein phosphatase 5 from Trypanosoma brucei.
pubmed:affiliation
Division of Microbial Pathogenesis and Immune Response, Department of Biomedical Sciences, Meharry Medical College, Nashville, Tennessee 37208, USA. mchaudhuri@mmc.edu
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural