Multiple protein kinase activities required for activation of sperm flagellar motility

1995 ◽  
Vol 32 (1) ◽  
pp. 65-79 ◽  
Author(s):  
Prem S. Chaudhry ◽  
Susan Creagh ◽  
Nam Yu ◽  
Charles J. Brokaw
Keyword(s):  
Protein Kinase ◽  
Flagellar Motility ◽  
Multiple Protein

scholarly journals Multiple protein kinase pathways mediate amplified IL-6 release by human lung fibroblasts co-exposed to nickel and TLR-2 agonist, MALP-2

2010 ◽  
Vol 247 (2) ◽  
pp. 146-157 ◽  
Author(s):  
Fei Gao ◽  
Kelly A. Brant ◽  
Rachel M. Ward ◽  
Richard T. Cattley ◽  
Aaron Barchowsky ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Human Lung ◽  
Lung Fibroblasts ◽  
Human Lung Fibroblasts ◽  
Multiple Protein

scholarly journals Protein Kinase C Is Likely to be Involved in Zoosporogenesis and Maintenance of Flagellar Motility in the Peronosporomycete Zoospores

2011 ◽  
Vol 24 (8) ◽  
pp. 938-947 ◽  
Author(s):  
Md. Tofazzal Islam ◽  
Andreas von Tiedemann ◽  
Hartmut Laatsch
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Downy Mildew ◽  
Kinase Inhibitors ◽  
Plasmopara Viticola ◽  
Active Principle ◽  
Dependent Manner ◽  
Flagellar Motility ◽  
Grapevine Downy Mildew ◽  
Kinase C

The motility of zoospores is critical in the disease cycles of Peronosporomycetes that cause devastating diseases in plants, fishes, vertebrates, and microbes. In the course of screening for secondary metabolites, we found that ethyl acetate extracts of a marine Streptomyces sp. strain B5136 rapidly impaired the motility of zoospores of the grapevine downy mildew pathogen Plasmopara viticola at 0.1 μg/ml. The active principle in the extracts was identified as staurosporine, a known broad-spectrum inhibitor of protein kinases, including protein kinase C (PKC). In the presence of staurosporine (2 nM), zoospores moved very slowly in their axis or spun in tight circles, instead of displaying straight swimming in a helical fashion. Compounds such as K-252a, K-252b, and K-252c structurally related to staurosporine also impaired the motility of zoospores in a similar manner but at varying doses. Among the 22 known kinase inhibitors tested, the PKC inhibitor chelerythrine was the most potent to arrest the motility of zoospores at concentrations starting from 5 nM. Inhibitors that targeted kinase pathways other than PKC pathways did not practically show any activity in impairing zoospore motility. Interestingly, both staurosporine (5 nM) and chelerythrine (10 nM) also inhibited the release of zoospores from the P. viticola sporangia in a dose-dependent manner. In addition, staurosporine completely suppressed downy mildew disease in grapevine leaves at 2 μM, suggesting the potential of small-molecule PKC inhibitors for the control of peronosporomycete phytopathogens. Taken together, these results suggest that PKC is likely to be a key signaling mediator associated with zoosporogenesis and the maintenance of flagellar motility in peronosporomycete zoospores.

Cell cycle-specific defects of flagellar motility upon reduced expression of a PKA-like protein kinase.

2005 ◽  
Vol 2005 (Fall) ◽  
Author(s):  
Michael Boshart ◽  
Carsten Krumbholz ◽  
Markus Engstler ◽  
Christoph G. Grünfelder
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Flagellar Motility

Convergence of Multiple Protein Kinase Pathways of Angiotensin II Type 1 Receptor on cAMP Response Element-Binding Protein (CREB) in Rat Vascular Smooth Muscle Cells

Hypertension ◽  
2000 ◽  
Vol 36 (suppl_1) ◽  
pp. 722-722
Author(s):  
Toshihiro Ichiki ◽  
Yuko Funakoshi ◽  
Kotaro Takeda ◽  
Akira Takeshita
Keyword(s):  
Smooth Muscle ◽  
Angiotensin Ii ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Gene Transcription ◽  
Interleukin 6 ◽  
Ang Ii ◽  
Creb Phosphorylation ◽  
Multiple Protein

P163 We previously reported a critical role of cyclic AMP response element (CRE) of interleukin-6 gene promoter in the induction of interleukin-6 gene expression by angiotensin II (AngII). We examined signaling pathways that are responsible for AngII-induced phosphorylation of CRE binding protein (CREB) at serine 133 that is a critical marker for the activation in rat vascular smooth muscle cells (VSMC). We performed Western blot analysis using an antibody against the phosphorylated form of CREB. AngII time-dependently induced phosphorylation of CREB with a peak at 5 minutes. The phosphorylation was dose-dependent. The AngII-induced phosphorylation of CREB was blocked by CV11974, an AngII type I receptor (AT1-R) antagonist but not by PD123319, an antagonist of Ang II type 2 receptor, suggesting that AT1-R mediates the phosphorylation of CREB. Inhibition of extracellular signal-regulated protein kinase (ERK) by PD98059 or inhibition of p38 mitogen activated protein kinase (MAPK) by SB203580 partially inhibited AngII-induced CREB phosphorylation. A protein kinase A (PKA) inhibitor, H89, also partially suppressed AngII-induced CREB phosphorylation. However, inhibition of calmodulin dependent kinase II or phosphatydilinositol 3 kinase did not affect Ang II-induced CREB phosphorylation. Transcriptional activation as measured by a CRE/luciferase reporter was increased by 1.7-fold by AngII stimulation. Infection of adenovirus vector expressing dominant negative form of CREB, which the serine residue at 133 is replaced with alanine to VSMC partially suppressed Ang II-induced thymidine incorporation. These findings suggest that AngII activates multiple protein kinase pathways involving two MAPK pathways and PKA, all of which contribute to the activation of CREB. And CREB-dependent gene transcription plays an important role for Ang II-induced mitogenesis. Activation of CREB-dependent gene transcription may play important roles in cardiovascular remodeling process.

scholarly journals CAK1 Promotes Meiosis and Spore Formation in Saccharomyces cerevisiae in a CDC28-Independent Fashion

2002 ◽  
Vol 22 (1) ◽  
pp. 57-68 ◽  
Author(s):  
Michael Schaber ◽  
Anne Lindgren ◽  
Karen Schindler ◽  
David Bungard ◽  
Philipp Kaldis ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Map Kinases ◽  
Spore Wall ◽  
Activation Loop ◽  
Multicopy Suppressor ◽  
Multiple Protein ◽  
Mitogen Activated Protein ◽  
Missense Mutant ◽  
Wall Assembly

ABSTRACT CAK1 encodes a protein kinase in Saccharomyces cerevisiae whose sole essential mitotic role is to activate the Cdc28p cyclin-dependent kinase by phosphorylation of threonine-169 in its activation loop. SMK1 encodes a sporulation-specific mitogen-activated protein (MAP) kinase homolog that is required to regulate the postmeiotic events of spore wall assembly. CAK1 was previously identified as a multicopy suppressor of a weakened smk1 mutant and shown to be required for spore wall assembly. Here we show that Smk1p, like other MAP kinases, is phosphorylated in its activation loop and that Smk1p is not activated in a cak1 missense mutant. Strains harboring a hyperactivated allele of CDC28 that is CAK1 independent and that lacks threonine-169 still require CAK1 to activate Smk1p. The data indicate that Cak1p functions upstream of Smk1p by activating a protein kinase other than Cdc28p. We also found that mutants lacking CAK1 are blocked early in meiotic development, as they show substantial delays in premeiotic DNA synthesis and defects in the expression of sporulation-specific genes, including IME1. The early meiotic role of Cak1p, like the postmeiotic role in the Smk1p pathway, is CDC28 independent. The data indicate that Cak1p activates multiple steps in meiotic development through multiple protein kinase targets.

scholarly journals Disruption of the A-Kinase Anchoring Domain in Flagellar Radial Spoke Protein 3 Results in Unregulated Axonemal cAMP-dependent Protein Kinase Activity and Abnormal Flagellar Motility

2006 ◽  
Vol 17 (6) ◽  
pp. 2626-2635 ◽  
Author(s):  
Anne R. Gaillard ◽  
Laura A. Fox ◽  
Jeanne M. Rhea ◽  
Branch Craige ◽  
Winfield S. Sale
Keyword(s):  
Protein Kinase ◽  
Physiological Role ◽  
Binding Domain ◽  
Cell Phenotype ◽  
Protein Kinase Activity ◽  
Flagellar Motility ◽  
Dependent Protein Kinase ◽  
Radial Spoke ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein

Biochemical studies of Chlamydomonas flagellar axonemes revealed that radial spoke protein (RSP) 3 is an A-kinase anchoring protein (AKAP). To determine the physiological role of PKA anchoring in the axoneme, an RSP3 mutant, pf14, was transformed with an RSP3 gene containing a mutation in the PKA-binding domain. Analysis of several independent transformants revealed that the transformed cells exhibit an unusual phenotype: a fraction of the cells swim normally; the remainder of the cells twitch feebly or are paralyzed. The abnormal/paralyzed motility is not due to an obvious deficiency of radial spoke assembly, and the phenotype cosegregates with the mutant RSP3. We postulated that paralysis was due to failure in targeting and regulation of axonemal cAMP-dependent protein kinase (PKA). To test this, reactivation experiments of demembranated cells were performed in the absence or presence of PKA inhibitors. Importantly, motility in reactivated cell models mimicked the live cell phenotype with nearly equal fractions of motile and paralyzed cells. PKA inhibitors resulted in a twofold increase in the number of motile cells, rescuing paralysis. These results confirm that flagellar RSP3 is an AKAP and reveal that a mutation in the PKA binding domain results in unregulated axonemal PKA activity and inhibition of normal motility.

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