YODA signalling in the early Arabidopsis embryo

2014 ◽  
Vol 42 (2) ◽  
pp. 408-412 ◽  
Author(s):  
Thomas J. Musielak ◽  
Martin Bayer
Keyword(s):  
Transcription Factors ◽  
Plant Hormone ◽  
Flowering Plants ◽  
Early Embryogenesis ◽  
Mitogen Activated Protein Kinase ◽  
Basal Cells ◽  
Cell Fates ◽  
Mitogen Activated Protein ◽  
Kinase Pathway

During early embryogenesis, flowering plants establish their principal body plan starting with an apical–basal axis. An asymmetric division of the zygote gives rise to apical and basal cells with different developmental fates. Besides WOX (WUSCHEL-RELATED HOMEOBOX) transcription factors and the plant hormone auxin, the YDA (YODA)/MAPK (mitogen-activated protein kinase) pathway plays a major role in establishing different cell fates after the first zygotic division. In the present review, we summarize the available data on YDA signalling during embryogenesis. The role of YDA in other developmental processes was taken into account to highlight possible implications for this pathway in the embryo.

scholarly journals Role of Mitogen-Activated Protein Kinase Pathway in Prostaglandin F2α-Induced Rat Puerperal Uterine Contraction

Endocrinology ◽  
1997 ◽  
Vol 138 (8) ◽  
pp. 3103-3111 ◽  
Author(s):  
Masahide Ohmichi ◽  
Koji Koike ◽  
Akiko Kimura ◽  
Kanji Masuhara ◽  
Hiromasa Ikegami ◽  
...  
Keyword(s):  
Map Kinase ◽  
Uterine Contraction ◽  
Prostaglandin F2α ◽  
Mek Inhibitor ◽  
Biological Action ◽  
Mitogen Activated Protein Kinase ◽  
Myometrial Cells ◽  
Mitogen Activated Protein ◽  
Kinase Pathway

Abstract In this study, prostaglandin (PG) F2α was found to activate mitogen-activated protein (MAP) kinase and MAP kinase kinase (MEK) in cultured rat puerperal uterine myometrial cells. PGF2α stimulation also led to an increase in phosphorylation of raf-1, son of sevenless (SOS), and Shc. Furthermore, we examined the mechanism by which PGF2α induced MAP kinase phosphorylation. Both pertussis toxin (10 ng/ml), which inactivates Gi/Go proteins, and expression of a peptide derived from the carboxyl terminus of the β-adrenergic receptor kinase 1 (βARK1), which specifically blocks signaling mediated by the βγ subunits of G proteins, blocked the PGF2α-induced activation of MAP kinase. Ritodrine (1 μm), which is known to relax uterine muscle contraction, attenuated PGF2α-induced tyrosine phosphorylation of MAP kinase. Moreover, to examine the role of MAP kinase pathway in uterine contraction, an inhibitor of MEK activity, PD098059, was used. Although MEK inhibitor had no effect on PGF2α-induced calcium mobilization, this inhibitor partially inhibited PGF2α-induced uterine contraction. These results provide evidence that PGF2α stimulates the MAP kinase signaling pathway in cultured rat puerperal uterine myometrial cells through Gβγ protein, suggesting that this new pathway may play an important role in the biological action of PGF2α on these cells.

scholarly journals Sti1 and Cdc37 Can Stabilize Hsp90 in Chaperone Complexes with a Protein Kinase

2004 ◽  
Vol 15 (4) ◽  
pp. 1785-1792 ◽  
Author(s):  
Paul Lee ◽  
Arsalan Shabbir ◽  
Christopher Cardozo ◽  
Avrom J. Caplan
Keyword(s):  
Protein Kinase ◽  
Kinase Domain ◽  
Mitogen Activated Protein Kinase ◽  
Protein Kinase Domain ◽  
Relative Contribution ◽  
Expression Studies ◽  
Mitogen Activated Protein ◽  
Gene Expression Studies ◽  
Kinase Pathway

Hsp90 functions in association with several cochaperones for folding of protein kinases and transcription factors, although the relative contribution of each to the overall reaction is unknown. We assayed the role of nine different cochaperones in the activation of Ste11, a Saccharomyces cerevisiae mitogen-activated protein kinase kinase kinase. Studies on signaling via this protein kinase pathway was measured by α-factor-stimulated induction of FIG1 or lacZ, and repression of HHF1. Several cochaperone mutants tested had reduced FIG1 induction or HHF1 repression, although to differing extents. The greatest defects were in cpr7Δ, sse1Δ, and ydj1Δ mutants. Assays of Ste11 kinase activity revealed a pattern of defects in the cochaperone mutant strains that were similar to the gene expression studies. Overexpression of CDC37, a chaperone required for protein kinase folding, suppressed defects the sti1Δ mutant back to wild-type levels. CDC37 overexpression also restored stable Hsp90 binding to the Ste11 protein kinase domain in the sti1Δ mutant strain. These data suggest that Cdc37 and Sti1 have functional overlap in stabilizing Hsp90:client complexes. Finally, we show that Cns1 functions in MAP kinase signaling in association with Cpr7.

Role of mitogen-activated protein kinase pathway in acetylcholine-mediated in vitro relaxation of rat pulmonary artery

2002 ◽  
Vol 434 (1-2) ◽  
pp. 55-64 ◽  
Author(s):  
Wai Yee Choy ◽  
Yung Fat Wong ◽  
Yiu Wa Kwan ◽  
Alice Lai Shan Au ◽  
Wing Hung Lau ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Pulmonary Artery ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Kinase Pathway
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