scholarly journals Combinatory action of VEGFR2 and MAP kinase pathways maintains endothelial-cell integrity

Cell Research ◽  
2011 ◽  
Vol 21 (7) ◽  
pp. 1080-1087 ◽  
Author(s):  
Hanbing Zhong ◽  
Danyang Wang ◽  
Nan Wang ◽  
Yesenia Rios ◽  
Haigen Huang ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Map Kinase ◽  
Cell Integrity ◽  
Map Kinase Pathways

scholarly journals A network of MAP-Kinase pathways and transcription factors regulates cell-to-cell communication and cell wall integrity in Neurospora crassa

2018 ◽  
Author(s):  
Monika S. Fischer ◽  
Vincent W. Wu ◽  
Ji E. Lee ◽  
Ronan C. O’Malley ◽  
N. Louise Glass
Keyword(s):  
Cell Wall ◽  
Transcription Factors ◽  
Map Kinase ◽  
Neurospora Crassa ◽  
Cell Fusion ◽  
Regulatory Network ◽  
Cell Communication ◽  
Cell Wall Integrity ◽  
Cell Integrity ◽  
Map Kinase Pathways

ABSTRACTMaintenance of cell integrity and cell-to-cell communication are fundamental biological processes. Filamentous fungi, such as Neurospora crassa, depend on communication to locate compatible cells, coordinate cell fusion, and establish a robust hyphal network. Two MAP-Kinase pathways are essential for communication and cell fusion in N. crassa; the Cell Wall Integrity/MAK-1 pathway and the MAK-2 (signal response) pathway. Previous studies have demonstrated several points of cross talk between the MAK-1 and MAK-2 pathways, which is likely necessary for oordinating chemotropic growth toward an extracellular signal, and then mediating cell fusion. Canonical MAP-Kinase pathways begin with signal reception and end with a transcriptional response. Two transcription factors, ADV-1 and PP-1, are essential for communication and cell fusion. PP-1 is the conserved target of MAK-2, while it is unclear what targets ADV-1. We did RNAseq on Δadv-1, Δpp-1, and wild-type cells and found that ADV-1 and PP-1 have a shared regulon including many genes required for communication, cell fusion, growth, development, and stress response. We identified ADV-1 and PP-1 binding sites across the genome by adapting the in vitro method of DNA-Affinity Purification sequencing (DAP-seq) for N. crassa. To elucidate the regulatory network, we misexpressed each transcription factor in each upstream MAPK deletion mutant. Misexpression of adv-1 was sufficient to fully suppress the phenotype of the Δpp-1 mutant and partially suppress the phenotype of the Δmak-1 mutant. Collectively, our data demonstrate that the MAK-1-ADV-1 and MAK-2- PP-1 pathways form a tight regulatory network that maintains cell integrity and mediates communication and cell fusion.

scholarly journals Differential involvement of NF-κB and MAP kinase pathways in the generation of inflammatory cytokines by human neutrophils

2006 ◽  
Vol 81 (2) ◽  
pp. 567-577 ◽  
Author(s):  
Alexandre Cloutier ◽  
Thornin Ear ◽  
Emilie Blais-Charron ◽  
Claire M. Dubois ◽  
Patrick P. McDonald
Keyword(s):  
Map Kinase ◽  
Inflammatory Cytokines ◽  
Human Neutrophils ◽  
Differential Involvement ◽  
Map Kinase Pathways

scholarly journals Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*

2001 ◽  
Vol 22 (2) ◽  
pp. 153-183 ◽  
Author(s):  
Gray Pearson ◽  
Fred Robinson ◽  
Tara Beers Gibson ◽  
Bing-e Xu ◽  
Mahesh Karandikar ◽  
...  
Keyword(s):  
Map Kinase ◽  
Physiological Functions ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Map Kinase Pathways

TOR and MAP kinase pathways synergistically regulate autophagy in response to nutrient depletion in fission yeast

Autophagy ◽  
2021 ◽  
pp. 1-16
Author(s):  
Cristina Corral-Ramos ◽  
Rubén Barrios ◽  
José Ayté ◽  
Elena Hidalgo
Keyword(s):  
Map Kinase ◽  
Fission Yeast ◽  
Nutrient Depletion ◽  
Map Kinase Pathways

Dual MAP kinase pathways mediate opposing forms of long-term plasticity at CA3–CA1 synapses

10.1038/80624 ◽  
2000 ◽  
Vol 3 (11) ◽  
pp. 1107-1112 ◽  
Author(s):  
V. Y. Bolshakov ◽  
L. Carboni ◽  
M.H. Cobb ◽  
S. A. Siegelbaum ◽  
F. Belardetti
Keyword(s):  
Map Kinase ◽  
Dual Map ◽  
Map Kinase Pathways

scholarly journals Expressed in the Yeast Saccharomyces cerevisiae, Human ERK5 Is a Client of the Hsp90 Chaperone That Complements Loss of the Slt2p (Mpk1p) Cell Integrity Stress-Activated Protein Kinase

2006 ◽  
Vol 5 (11) ◽  
pp. 1914-1924 ◽  
Author(s):  
Andrew W. Truman ◽  
Stefan H. Millson ◽  
James M. Nuttall ◽  
Victoria King ◽  
Mehdi Mollapour ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Map Kinase ◽  
Protein Kinases ◽  
Strong Association ◽  
Active Form ◽  
Cell Integrity ◽  
Binding Studies ◽  
Hsp90 Inhibition ◽  
Binding Surface ◽  
Hsp90 Chaperone

ABSTRACT ERK5 is a mitogen-activated protein (MAP) kinase regulated in human cells by diverse mitogens and stresses but also suspected of mediating the effects of a number of oncogenes. Its expression in the slt2Δ Saccharomyces cerevisiae mutant rescued several of the phenotypes caused by the lack of Slt2p (Mpk1p) cell integrity MAP kinase. ERK5 is able to provide this cell integrity MAP kinase function in yeast, as it is activated by the cell integrity signaling cascade that normally activates Slt2p and, in its active form, able to stimulate at least one key Slt2p target (Rlm1p, the major transcriptional regulator of cell wall genes). In vitro ERK5 kinase activity was abolished by Hsp90 inhibition. ERK5 activity in vivo was also lost in a strain that expresses a mutant Hsp90 chaperone. Therefore, human ERK5 expressed in yeast is an Hsp90 client, despite the widely held belief that the protein kinases of the MAP kinase class are non-Hsp90-dependent activities. Two-hybrid and protein binding studies revealed that strong association of Hsp90 with ERK5 requires the dual phosphorylation of the TEY motif in the MAP kinase activation loop. These phosphorylations, at positions adjacent to the Hsp90-binding surface recently identified for a number of protein kinases, may cause a localized rearrangement of this MAP kinase region that leads to creation of the Hsp90-binding surface. Complementation of the slt2Δ yeast defect by ERK5 expression establishes a new tool with which to screen for novel agonists and antagonists of ERK5 signaling as well as for isolating mutant forms of ERK5.

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