Linked Life Data

19837628

Source:http://linkedlifedata.com/resource/pubmed/id/19837628

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2009-11-17
pubmed:abstractText
Fungal cells exist in a diverse range of morphologies. Some species, such as Candida albicans, are dimorphic capable of growing either in a yeast-like form or as a hypha. Cyclin-dependent kinases (CDKs) have long been thought to play a central role in the yeast-hyphal decision. However, until recently direct links of CDKs with proteins that execute polarized growth were elusive. In this review I will focus on new findings that have established concrete links between CDKs and several key components of the polarity machinery in C. albicans and the budding yeast Saccharomyces cerevisiae. Inhibitory phosphorylation of the GTPase-activating proteins (GAPs) of Cdc42 has emerged as a common mechanism underlying polarized growth in both organisms. C. albicans contains a hyphal-specific cyclin Hgc1. In association with the CDK Cdc28 it ensures hyphal development by phosphorylating the Cdc42 GAP Rga2, two septins and the transcription factor Efg1. This review will discuss both conserved mechanisms and ones specific for hyphal development in C. albicans.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1879-0364
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
644-9
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
CDKs and the yeast-hyphal decision.
pubmed:affiliation
Genes and Development Division, Institute of Molecular and Cell Biology, 61 Biopolis Drive, Singapore 138673, Singapore. mcbwangy@imcb.a-star.edu.sg
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't