Critical Determinants of Substrate Recognition by Cyclin-Dependent Kinase-like 5 (CDKL5)

Biochemistry ◽  
2015 ◽  
Vol 54 (19) ◽  
pp. 2975-2987 ◽  
Author(s):  
Syouichi Katayama ◽  
Noriyuki Sueyoshi ◽  
Isamu Kameshita
Keyword(s):  
Substrate Recognition ◽  
Cyclin Dependent Kinase

scholarly journals Structure-function relationships of the yeast cyclin-dependent kinase Pho85.

1995 ◽  
Vol 15 (10) ◽  
pp. 5482-5491 ◽  
Author(s):  
R C Santos ◽  
N C Waters ◽  
C L Creasy ◽  
L W Bergman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Structure Function ◽  
Cell Cycle Progression ◽  
Substrate Recognition ◽  
The Other ◽  
Cyclin Dependent Kinase ◽  
Cycle Progression ◽  
Cyclin Dependent Kinases ◽  
Induced Mutagenesis

The PHO85 gene of Saccharomyces cerevisiae encodes a cyclin-dependent kinase involved in both transcriptional regulation and cell cycle progression. Although a great deal is known concerning the structure, function, and regulation of the highly homologous Cdc28 protein kinase, little is known concerning these relationships in regard to Pho85. In this study, we constructed a series of Pho85-Cdc28 chimeras to map the region(s) of the Pho85 molecule that is critical for function of Pho85 in repression of acid phosphatase (PHO5) expression. Using a combination of site-directed and ethyl methanesulfonate-induced mutagenesis, we have identified numerous residues critical for either activation of the Pho85 kinase, interaction of Pho85 with the cyclin-like molecule Pho80, or substrate recognition. Finally, analysis of mutations analogous to those previously identified in either Cdc28 or cdc2 of Schizosaccharomyces pombe suggested that the inhibition of Pho85-Pho80 activity in mechanistically different from that seen in the other cyclin-dependent kinases.

scholarly journals Autophosphorylation-Induced Degradation of the Pho85 Cyclin Pcl5 Is Essential for Response to Amino Acid Limitation

2008 ◽  
Vol 28 (22) ◽  
pp. 6858-6869 ◽  
Author(s):  
Sharon Aviram ◽  
Einav Simon ◽  
Tsvia Gildor ◽  
Fabian Glaser ◽  
Daniel Kornitzer
Keyword(s):  
Amino Acid ◽  
Ubiquitin Ligase ◽  
Substrate Recognition ◽  
Amino Acid Starvation ◽  
Cyclin Dependent Kinase ◽  
Threonine Residue ◽  
The Core ◽  
Recognition Function ◽  
Scf Ubiquitin Ligase

ABSTRACT Pho85 cyclins (Pcls), activators of the yeast cyclin-dependent kinase (CDK) Pho85, belong together with the p35 activator of mammalian CDK5 to a distinct structural cyclin class. Different Pcls target Pho85 to distinct substrates. Pcl5 targets Pho85 specifically to Gcn4, a yeast transcription factor involved in the response to amino acid starvation, eventually causing the degradation of Gcn4. Pcl5 is itself highly unstable, an instability that was postulated to be important for regulation of Gcn4 degradation. We used hybrids between different Pcls to circumscribe the substrate recognition function to the core cyclin box domain of Pcl5. Furthermore, the cyclin hybrids revealed that Pcl5 degradation is uniquely dependent on two distinct degradation signals: one N-terminal and one C-terminal to the cyclin box domain. Whereas the C-terminal degradation signal is independent of Pho85, the N-terminal degradation signal requires phosphorylation of a specific threonine residue by the Pho85 molecule bound to the cyclin. This latter mode of degradation depends on the SCF ubiquitin ligase. Degradation of Pcl5 after self-catalyzed phosphorylation ensures that activity of the Pho85/Pcl5 complex is self-limiting in vivo. We demonstrate the importance of this mechanism for the regulation of Gcn4 degradation and for cell growth under conditions of amino acid starvation.

Site-Specific Phosphorylation of Lys-Ser-Pro Repeat Peptides from Neurofilament H by Cyclin-Dependent Kinase 5:  Structural Basis for Substrate Recognition

Biochemistry ◽  
1998 ◽  
Vol 37 (14) ◽  
pp. 4759-4766 ◽  
Author(s):  
Pushkar Sharma ◽  
Joseph J. Barchi, ◽  
Xiaolin Huang ◽  
Niranjana D. Amin ◽  
Howard Jaffe ◽  
...  
Keyword(s):  
Substrate Recognition ◽  
Structural Basis ◽  
Cyclin Dependent Kinase ◽  
Site Specific ◽  
Cyclin Dependent Kinase 5

scholarly journals Cyclin-Cyclin-dependent Kinase Regulatory Response Is Linked to Substrate Recognition

2011 ◽  
Vol 286 (11) ◽  
pp. 9713-9725
Author(s):  
Maria Emanuela Cuomo ◽  
Georgina M. Platt ◽  
Laurence H. Pearl ◽  
Sibylle Mittnacht
Keyword(s):  
Substrate Recognition ◽  
Cyclin Dependent Kinase ◽  
Regulatory Response

Hypoxic preconditioning reduces expression of the cyclin dependent kinase 5 in the post-ischemic neurons

2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S309-S309
Author(s):  
Svetlana Pundik ◽  
W David Lust ◽  
Jose Valerio ◽  
Michael Buczek ◽  
Randall D York ◽  
...  
Keyword(s):  
Hypoxic Preconditioning ◽  
Cyclin Dependent Kinase ◽  
Cyclin Dependent Kinase 5

Substrate Recognition by Vitamin K-Dependent Carboxylase

1987 ◽  
Vol 57 (01) ◽  
pp. 017-019 ◽  
Author(s):  
Magda M W Ulrich ◽  
Berry A M Soute ◽  
L Johan M van Haarlem ◽  
Cees Vermeer
Keyword(s):  
Amino Acid ◽  
Vitamin K ◽  
Substrate Recognition ◽  
Bovine Liver ◽  
Amino Acid Residues

SummaryDecarboxylated osteocalcins were prepared and purified from bovine, chicken, human and monkey bones and assayed for their ability to serve as a substrate for vitamin K-dependent carboxylase from bovine liver. Substantial differences were observed, especially between bovine and monkey d-osteocalcin. Since these substrates differ only in their amino acid residues 3 and 4, it seems that these residues play a role in the recognition of a substrate by hepatic carboxylase.

Sign in / Sign up

Export Citation Format

Share Document