scholarly journals A Comprehensive Phylogenetic Analysis of the MAP4K Family in the Green Lineage

2021 ◽  
Vol 12 ◽  
Author(s):  
Lixia Pan ◽  
Cassio Flavio Fonseca De Lima ◽  
Lam Dai Vu ◽  
Ive De Smet
Keyword(s):  
Green Algae ◽  
Phylogenetic Reconstruction ◽  
Mitogen Activated Protein Kinase ◽  
Comprehensive Overview ◽  
Representative Species ◽  
Evolutionarily Conserved ◽  
Mitogen Activated Protein ◽  
Green Lineage ◽  
Basic Cellular Process

The kinase-mediated phosphorylation impacts every basic cellular process. While mitogen-activated protein kinase technology kinase kinases (MAP4Ks) are evolutionarily conserved, there is no comprehensive overview of the MAP4K family in the green lineage (Viridiplantae). In this study, we identified putative MAP4K members from representative species of the two core groups in the green lineage: Chlorophyta, which is a diverse group of green algae, and Streptophyta, which is mostly freshwater green algae and land plants. From that, we inferred the evolutionary relationships of MAP4K proteins through a phylogenetic reconstruction. Furthermore, we provided a classification of the MAP4Ks in the green lineage into three distinct.

scholarly journals Identification of Cdc37 as a Novel Regulator of the Stress-Responsive Mitogen-Activated Protein Kinase

2003 ◽  
Vol 23 (15) ◽  
pp. 5132-5142 ◽  
Author(s):  
Hisashi Tatebe ◽  
Kazuhiro Shiozaki
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Inflammatory Responses ◽  
Cellular Level ◽  
Mitogen Activated Protein Kinase ◽  
Cellular Survival ◽  
Evolutionarily Conserved ◽  
Mitogen Activated Protein ◽  
Extracellular Stimuli ◽  
The Stability

ABSTRACT Eukaryotic cells utilize multiple mitogen-activated protein kinases (MAPKs) to transmit various extracellular stimuli to the nucleus. A subfamily of MAPKs that mediates environmental stress stimuli is also called stress-activated protein kinase (SAPK), which has crucial roles in cellular survival under stress conditions as well as inflammatory responses. Here we report that Cdc37, an evolutionarily conserved kinase-specific chaperone, is a positive regulator of Spc1 SAPK in the fission yeast Schizosaccharomyces pombe. Through a genetic screen, we have identified cdc37 as a mutation that compromises signaling through Spc1 SAPK. The Cdc37 protein physically interacts with Spc1, and the cdc37 mutation affects both the cellular level of the Spc1 protein and stress-induced Spc1 phosphorylation by Wis1 MAPK kinase (MAPKK). Consistently, expression of the stress response genes regulated by the Spc1 pathway is compromised in cdc37 mutant cells. On the other hand, a mutation in Hsp90, which often cooperates with Cdc37 in chaperoning protein kinases, does not affect Spc1 SAPK. These results suggest that Spc1 SAPK is a novel client protein for the Cdc37 chaperone, and the Cdc37 function is important to maintain the stability of the Spc1 protein and to facilitate stress signaling from Wis1 MAPKK to Spc1 SAPK.

scholarly journals Sin1-mediated mTOR signaling in cell growth, metabolism and immune response

2019 ◽  
Vol 6 (6) ◽  
pp. 1149-1162
Author(s):  
Chun Ruan ◽  
Xinxing Ouyang ◽  
Hongzhi Liu ◽  
Song Li ◽  
Jingsi Jin ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Current Knowledge ◽  
Mammalian Target Of Rapamycin ◽  
Adaptor Protein ◽  
Interaction Network ◽  
Mitogen Activated Protein Kinase ◽  
Cellular Functions ◽  
Evolutionarily Conserved ◽  
Mitogen Activated Protein ◽  
Growth Metabolism

Abstract The mammalian target of rapamycin (mTOR) is an evolutionarily conserved Ser/Thr protein kinase with essential cellular function via processing various extracellular and intracellular inputs. Two distinct multi-protein mTOR complexes (mTORC), mTORC1 and mTORC2, have been identified and well characterized in eukaryotic cells from yeast to human. Sin1, which stands for Sty1/Spc1-interacting protein1, also known as mitogen-activated protein kinase (MAPK) associated protein (MAPKAP)1, is an evolutionarily conserved adaptor protein. Mammalian Sin1 interacts with many cellular proteins, but it has been widely studied as an essential component of mTORC2, and it is crucial not only for the assembly of mTORC2 but also for the regulation of its substrate specificity. In this review, we summarize our current knowledge of the structure and functions of Sin1, focusing specifically on its protein interaction network and its roles in the mTOR pathway that could account for various cellular functions of mTOR in growth, metabolism, immunity and cancer.

scholarly journals Identification of green lineage osmotic stress pathways

2021 ◽  
Author(s):  
Josep Vilarrasa-Blasi ◽  
Tamara Vellosillo ◽  
Robert E. Jinkerson ◽  
Friedrich Fauser ◽  
Tingting Xiang ◽  
...  
Keyword(s):  
Osmotic Stress ◽  
Stress Tolerance ◽  
Land Plant ◽  
Mitogen Activated Protein Kinase ◽  
Stress Signaling ◽  
Osmotic Stress Tolerance ◽  
Mitogen Activated Protein ◽  
Transport Vesicle ◽  
Living Organisms ◽  
Green Lineage

Maintenance of water homeostasis is a fundamental cellular process required by all living organisms. Here, we use the green alga Chlamydomonas reinhardtii to establish a foundational understanding of evolutionarily conserved osmotic-stress signaling pathways in the green lineage through transcriptomics, phosphoproteomics, and functional genomics approaches. Five genes acting across diverse cellular pathways were found to be essential for osmotic-stress tolerance in Chlamydomonas including cytoskeletal organization, potassium transport, vesicle trafficking, mitogen-activated protein kinase and chloroplast signaling. We show that homologs of these genes in the multicellular land plant Arabidopsis thaliana have conserved functional roles in stress tolerance and reveal a novel PROFILIN-dependent actin remodeling stage of acclimation that ensures cell survival and tissue integrity upon osmotic stress. This study highlights the conservation of the stress response in algae and land plants and establishes Chlamydomonas as a unicellular plant model system to dissect the osmotic stress signaling pathway.

scholarly journals Schizosaccharomyces pombe Spk1 is a tyrosine-phosphorylated protein functionally related to Xenopus mitogen-activated protein kinase.

1993 ◽  
Vol 13 (10) ◽  
pp. 6427-6434 ◽  
Author(s):  
Y Gotoh ◽  
E Nishida ◽  
M Shimanuki ◽  
T Toda ◽  
Y Imai ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Schizosaccharomyces Pombe ◽  
Tyrosine Phosphorylation ◽  
Mitogen Activated Protein Kinase ◽  
Diploid Strain ◽  
Evolutionarily Conserved ◽  
Mitogen Activated Protein ◽  
Tyrosine Phosphorylated Protein ◽  
Higher Eukaryotes ◽  
Direct Activator

Mitogen-activated protein kinase (MAPK) and its direct activator, MAPK kinase (MAPKK), have been suggested to play a pivotal role in a variety of signal transduction pathways in higher eukaryotes. The fission yeast Schizosaccharomyces pombe carries a gene, named spk1, whose product is structurally related to vertebrate MAPK. Here we show that Spk1 is functionally related to Xenopus MAPK. (i) Xenopus MAPK partially complemented a defect in the spk1- mutant. An spk1- diploid strain could not sporulate, but one carrying Xenopus MAPK could. (ii) Both Spk1 and Xenopus MAPK interfered with sporulation if overexpressed in S. pombe cells. (iii) Spk1 underwent tyrosine phosphorylation as does Xenopus MAPK. Tyrosine phosphorylation of Spk1 appeared to be dependent upon mating signals because it occurred in homothallic cells but not in heterothallic cells. Furthermore, this phosphorylation was diminished in a byr1 disruptant strain, suggesting that spk1 lies downstream of byr1, which encodes a MAPKK homolog in S. pombe. Taken together, the MAPKK-MAPK cascade may be evolutionarily conserved in signaling pathways in yeasts and vertebrates.

scholarly journals Mitogen-Activated Protein Kinase Signaling in the Heart: Angels Versus Demons in a Heart-Breaking Tale

2010 ◽  
Vol 90 (4) ◽  
pp. 1507-1546 ◽  
Author(s):  
Beth A. Rose ◽  
Thomas Force ◽  
Yibin Wang
Keyword(s):  
Intracellular Signaling ◽  
Cardiac Development ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Mitogen Activated Protein Kinase ◽  
Comprehensive Overview ◽  
Primary Object ◽  
Critical Issues ◽  
Mitogen Activated Protein ◽  
Therapeutic Development

Among the myriad of intracellular signaling networks that govern the cardiac development and pathogenesis, mitogen-activated protein kinases (MAPKs) are prominent players that have been the focus of extensive investigations in the past decades. The four best characterized MAPK subfamilies, ERK1/2, JNK, p38, and ERK5, are the targets of pharmacological and genetic manipulations to uncover their roles in cardiac development, function, and diseases. However, information reported in the literature from these efforts has not yet resulted in a clear view about the roles of specific MAPK pathways in heart. Rather, controversies from contradictive results have led to a perception that MAPKs are ambiguous characters in heart with both protective and detrimental effects. The primary object of this review is to provide a comprehensive overview of the current progress, in an effort to highlight the areas where consensus is established verses the ones where controversy remains. MAPKs in cardiac development, cardiac hypertrophy, ischemia/reperfusion injury, and pathological remodeling are the main focuses of this review as these represent the most critical issues for evaluating MAPKs as viable targets of therapeutic development. The studies presented in this review will help to reveal the major challenges in the field and the limitations of current approaches and point to a critical need in future studies to gain better understanding of the fundamental mechanisms of MAPK function and regulation in the heart.

scholarly journals Defining the Molecular Genetics of Dermoscopic Naevus Patterns

Dermatology ◽  
2018 ◽  
Vol 235 (1) ◽  
pp. 19-34 ◽  
Author(s):  
Jean-Marie Tan ◽  
Lisa N. Tom ◽  
H. Peter Soyer ◽  
Mitchell S. Stark
Keyword(s):  
Protein Kinase ◽  
Cutaneous Melanoma ◽  
Somatic Mutations ◽  
Mitogen Activated Protein Kinase ◽  
Genomic Correlation ◽  
Mitogen Activated Protein ◽  
Somatic Alterations ◽  
Melanocytic Naevi ◽  
Kinase Pathway

Melanocytic naevi are common melanocytic proliferations that may simulate the appearance of cutaneous melanoma. Naevi commonly harbour somatic mutations implicated in melanomagenesis but in most cases lack the necessary genomic alterations required for melanoma development. While the mitogen-activated protein kinase pathway and ultraviolet radiation strongly contribute to naevogenesis, the somatic mutational landscape of dermoscopic naevus subsets distinguishes some of the molecular hallmarks of naevi in relation to melanoma. We herein discuss the classification of naevi and theories of naevogenesis and review the current literature on the somatic alterations in naevi and melanoma. This review focusses on the clinical-dermoscopic-pathological and genomic correlation of naevi that shapes the current understanding of naevi.

scholarly journals Inhibitor-2 induced M-phase arrest in Xenopus cycling egg extracts is dependent on MAPK activation

2011 ◽  
Vol 16 (4) ◽  
Author(s):  
Arian Khandani ◽  
Mahmood Mohtashami ◽  
Anne Camirand
Keyword(s):  
Cell Cycle ◽  
Mapk Pathway ◽  
Mitogen Activated Protein Kinase ◽  
Protein Phosphatase 1 ◽  
Mapk Activity ◽  
Phase Arrest ◽  
Evolutionarily Conserved ◽  
M Phase ◽  
Egg Extracts ◽  
Mitogen Activated Protein

AbstractThe evolutionarily-conserved protein phosphatase 1 (PP1) plays a central role in dephosphorylation of phosphoproteins during the M phase of the cell cycle. We demonstrate here that the PP1 inhibitor inhibitor-2 protein (Inh-2) induces an M-phase arrest in Xenopus cycling egg extracts. Interestingly, the characteristics of this M-phase arrest are similar to those of mitogen-activated protein kinase (p42MAPK)-induced M-phase arrest. This prompted us to investigate whether Inh-2-induced M-phase arrest was dependent on activation of the p42MAPK pathway. We demonstrate here that MAPK activity is required for Inh-2-induced M-phase arrest, as inhibition of MAPK by PD98059 allowed cycling extracts to exit M phase, despite the presence of Inh-2. We next investigated whether Inh-2 phosphorylation by the MAPK pathway was required to induce an M-phase arrest. We discovered that while p90Rsk (a MAPK protein required for M-phase arrest) is able to phosphorylate Inh-2, this phosphorylation is not required for Inh-2 function. Overall, our results suggest a novel mechanism linking p42MAPK and PP1 pathways during M phase of the cell cycle.

scholarly journals PsSAK1, a Stress-Activated MAP Kinase of Phytophthora sojae, Is Required for Zoospore Viability and Infection of Soybean

2010 ◽  
Vol 23 (8) ◽  
pp. 1022-1031 ◽  
Author(s):  
Aining Li ◽  
Yonglin Wang ◽  
Kai Tao ◽  
Suomeng Dong ◽  
Qian Huang ◽  
...  
Keyword(s):  
Hyphal Growth ◽  
Polymerase Chain Reaction Analysis ◽  
Phytophthora Sojae ◽  
Mitogen Activated Protein Kinase ◽  
Pleckstrin Homology Domain ◽  
Evolutionarily Conserved ◽  
Mitogen Activated Protein ◽  
Important Regulator ◽  
Soybean Leaves ◽  
Germ Tubes

Mitogen-activated protein kinase (MAPK) pathways are universal and evolutionarily conserved signal transduction modules in all eukaryotic cells. In this study, PsSAK1, which encodes a stress-activated MAPK of Phytophthora sojae, was identified. PsSAK1 is highly conserved in oomycetes, and it represents a novel group of MAPK due to its pleckstrin homology domain. Reverse-transcription polymerase chain reaction analysis showed that PsSAK1 expression was upregulated in zoospores and cysts and during early infection. In addition, its expression was induced by osmotic and oxidative stress mediated by NaCl and H2O2, respectively. To elucidate the function, the expression of PsSAK1 was silenced using stable transformation of P. sojae. The silencing of PsSAK1 did not impair hyphal growth, sporulation, or oospore production but severely hindered zoospore development, in that the silenced strains showed quicker encystment and a lower germination ratio than the wild type. PsSAK1-silenced mutants produced much longer germ tubes and could not colonize either wounded or unwounded soybean leaves. Our results indicate that PsSAK1 is an important regulator of zoospore development and pathogenicity in P. sojae.

Dermatoskopie: Naevi besser verstehen

2019 ◽  
Vol 7 (3) ◽  
pp. 120-121
Author(s):  
Max Schlaak
Keyword(s):  
Protein Kinase ◽  
Cutaneous Melanoma ◽  
Somatic Mutations ◽  
Mitogen Activated Protein Kinase ◽  
Genomic Correlation ◽  
Mitogen Activated Protein ◽  
Somatic Alterations ◽  
Melanocytic Naevi ◽  
Kinase Pathway

Melanocytic naevi are common melanocytic proliferations that may simulate the appearance of cutaneous melanoma. Naevi commonly harbour somatic mutations implicated in melanomagenesis but in most cases lack the necessary genomic alterations required for melanoma development. While the mitogen-activated protein kinase pathway and ultraviolet radiation strongly contribute to naevogenesis, the somatic mutational landscape of dermoscopic naevus subsets distinguishes some of the molecular hallmarks of naevi in relation to melanoma. We herein discuss the classification of naevi and theories of naevogenesis and review the current literature on the somatic alterations in naevi and melanoma. This review focusses on the clinical-dermoscopic-pathological and genomic correlation of naevi that shapes the current understanding of naevi.

scholarly journals The interaction of p38 with its upstream kinase MKK6

2020 ◽  
Author(s):  
Ganesan Senthil Kumar ◽  
Rebecca Page ◽  
Wolfgang Peti
Keyword(s):  
Cellular Response ◽  
Mitogen Activated Protein Kinase ◽  
Titration Calorimetry ◽  
Structural Element ◽  
Binding Interface ◽  
Evolutionarily Conserved ◽  
Mitogen Activated Protein ◽  
Upstream Kinase ◽  
Mapk Phosphatases ◽  
Extracellular Stimuli

ABSTRACTMitogen-activated protein kinase (MAPK; p38, ERK and JNK) cascades are evolutionarily conserved signaling pathways that regulate the cellular response to a variety of extracellular stimuli, such as growth factors and interleukins. The MAPK p38 is activated by its specific upstream MAPK kinases, MKK6 and MKK3. However, a comprehensive molecular understanding of how these cognate upstream kinases bind and activate p38 is still missing. Here, we combine NMR spectroscopy and isothermal titration calorimetry to define the binding interface between full-length MKK6 and p38. We show that p38 engages MKK6 not only via its hydrophobic docking groove, but also helix αF, a secondary structural element that plays a key role in organizing the kinase core. We also show that, unlike MAPK phosphatases, the p38 conserved docking (CD) site is much less affected by MKK6 binding. Finally, we demonstrate that these interactions with p38 are conserved independent of the MKK6 activation state. Together, our results reveal differences between specificity markers of p38 regulation by upstream kinases, which do not effectively engage the CD site, and downstream phosphatases, which require the CD site for productive binding.

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