Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.11.22 (cdc2)
 8,319 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To understand the genetic control of algal cell division cycle that pertains to phytoplankton bloom dynamics in the sea, we cloned and analyzed a gene coding for a cyclin-dependent kinase (CDK) for the chlorophyte Dunaliella tertiolecta. The cDNA cloned, 1061 bp long, contained an open reading frame of 314 amino acids. FASTA and GAP analyses showed that this sequence was most homologous to cdc2 out of all known cdks, with an identity of 54-68% and a similarity of 65-76% to cdc2 in higher plants, animals, and yeast. Several signature domains of cdc2 were identified from this sequence, although the PSTAIRE and GDSEID motifs were replaced with PSTTLRE and GDCELQ, respectively. Southern blot hybridization demonstrated that this gene occurred as a single copy in this species, and quantitative RT-PCR showed that the transcription of this gene was constitutive. The present results suggest that the universal cdc2 is conserved in the lower eukaryote with unique structural characteristics.
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PMID:A PSTTLRE-form of cdc2-like gene in the marine microalga Dunaliella tertiolecta. 1057 Oct 32

Site-specific activation of the Rho-type GTPase Cdc42p is critical for the establishment of cell polarity. Here we investigated the role and regulation of the GTPase-activating enzymes (GAPs) Bem2p and Bem3p for Cdc42p activation and actin polarization at bud emergence in Saccharomyces cerevisiae. Bem2p and Bem3p are localized throughout the cytoplasm and the cell cortex in unbudded G1 cells, but accumulate at sites of polarization after bud emergence. Inactivation of Bem2p results in hyperactivation of Cdc42p and polarization toward multiple sites. Bem2p and Bem3p are hyperphosphorylated at bud emergence most likely by the Cdc28p-Cln2p kinase. This phosphorylation appears to inhibit their GAP activity in vivo, as non-phosphorylatable Bem3p mutants are hyperactive and interfere with Cdc42p activation. Taken together, our results indicate that Bem2p and Bem3p may function as global inhibitors of Cdc42p activation during G1, and their inactivation by the Cdc28p/Cln kinase contributes to site-specific activation of Cdc42p at bud emergence.
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PMID:Phosphorylation of Bem2p and Bem3p may contribute to local activation of Cdc42p at bud emergence. 1791 57

Centralspindlin, a complex composed of the subunits ZEN-4 and CYK-4, recruits and regulates proteins that modulate the actin cytoskeleton to promote cleavage furrow formation and progression during cytokinesis. The ZEN-4 subunit is a kinesin that is proposed to function primarily by bundling microtubules and promoting transport of the complex to the midzone. ZEN-4 and CYK-4 are mutually dependent for localization to the midzone during cytokinesis. Once at the midzone, the CYK-4 subunit functions to recruit actin regulators and the scaffold anillin as well as to regulate RhoA and Rac via its intrinsic GAP domain, ultimately promoting actomyosin contractile ring assembly. We have revealed a distinct mechanism for centralspindlin localization and function at a stable, postmitotic intercellular bridge in the Caenorhabditis elegans gonad. Loss of zen-4 or cyk-4 function disrupts germ cell progression postmitotically. In contrast to the localization and recruitment relationships during mitosis, centralspindlin is maintained at the intercellular bridge by anillin, and CYK-4 is localized independently of ZEN-4 but not vice versa. We present evidence that centralspindlin function at the rachis bridge involves ZEN-4 action on the microtubules as opposed to the regulation of the actin cytoskeleton mediated by CYK-4 during cytokinesis.
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PMID:A postmitotic function and distinct localization mechanism for centralspindlin at a stable intercellular bridge. 2337 Jan 48