6dtl
From Proteopedia
(Difference between revisions)
| Line 10: | Line 10: | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/MPK6_ARATH MPK6_ARATH]] Involved in oxidative stress-mediated signaling cascade (such as ozone). Involved in the innate immune MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6) downstream of bacterial flagellin receptor FLS2. May be involved in hypersensitive response (HR)-mediated signaling cascade by modulating LIP5 phosphorylation and subsequent multivesicular bodies (MVBs) trafficking. May phosphorylate regulators of WRKY transcription factors. Phosphorylates 1-aminocyclopropane-1-carboxylic acid synthases (ACS2 and ACS6) and may be involved in the regulation of bacterial elicitor flagellin-induced ethylene production. Regulates locally gene-mediated and basal resistance response to certain pathogens. May be involved in the cold and salinity stress-mediated MAP kinase signaling cascade (MEKK1, MKK1/MKK2 and MPK4/MPK6). MKK1-MPK6 module mediates abscisic acid (ABA)-dependent CAT1 expression with H(2)O(2) production and response to drought and salt stress. MKK1-MPK6 module is also involved in sugar signaling during the process of seed germination. MKK3-MPK6 module plays an important role in the jasmonate signal transduction pathway through the negative regulation of MYC2/JIN1 expression. MKK9-MPK3/MPK6 module phosphorylates and activates EIN3, leading to the promotion of EIN3-mediated transcription in ethylene signaling. MPK3/MPK6 cascade regulates camalexin synthesis through transcriptional regulation of the biosynthetic genes after pathogen infection. MKK9-MPK6 module positively regulates leaf senescence. YDA-MKK4/MKK5-MPK3/MPK6 module regulates stomatal cell fate before the guard mother cell (GMC) is specified. This MAPK cascade also functions downstream of the ER receptor in regulating coordinated local cell proliferation, which shapes the morphology of plant organs.<ref>PMID:11875555</ref> <ref>PMID:15020743</ref> <ref>PMID:15225555</ref> <ref>PMID:15539472</ref> <ref>PMID:15964670</ref> <ref>PMID:17259259</ref> <ref>PMID:17369371</ref> <ref>PMID:18248592</ref> <ref>PMID:18273012</ref> <ref>PMID:18378893</ref> <ref>PMID:19251906</ref> <ref>PMID:19484493</ref> <ref>PMID:23263767</ref> <ref>PMID:25010425</ref> | [[http://www.uniprot.org/uniprot/MPK6_ARATH MPK6_ARATH]] Involved in oxidative stress-mediated signaling cascade (such as ozone). Involved in the innate immune MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6) downstream of bacterial flagellin receptor FLS2. May be involved in hypersensitive response (HR)-mediated signaling cascade by modulating LIP5 phosphorylation and subsequent multivesicular bodies (MVBs) trafficking. May phosphorylate regulators of WRKY transcription factors. Phosphorylates 1-aminocyclopropane-1-carboxylic acid synthases (ACS2 and ACS6) and may be involved in the regulation of bacterial elicitor flagellin-induced ethylene production. Regulates locally gene-mediated and basal resistance response to certain pathogens. May be involved in the cold and salinity stress-mediated MAP kinase signaling cascade (MEKK1, MKK1/MKK2 and MPK4/MPK6). MKK1-MPK6 module mediates abscisic acid (ABA)-dependent CAT1 expression with H(2)O(2) production and response to drought and salt stress. MKK1-MPK6 module is also involved in sugar signaling during the process of seed germination. MKK3-MPK6 module plays an important role in the jasmonate signal transduction pathway through the negative regulation of MYC2/JIN1 expression. MKK9-MPK3/MPK6 module phosphorylates and activates EIN3, leading to the promotion of EIN3-mediated transcription in ethylene signaling. MPK3/MPK6 cascade regulates camalexin synthesis through transcriptional regulation of the biosynthetic genes after pathogen infection. MKK9-MPK6 module positively regulates leaf senescence. YDA-MKK4/MKK5-MPK3/MPK6 module regulates stomatal cell fate before the guard mother cell (GMC) is specified. This MAPK cascade also functions downstream of the ER receptor in regulating coordinated local cell proliferation, which shapes the morphology of plant organs.<ref>PMID:11875555</ref> <ref>PMID:15020743</ref> <ref>PMID:15225555</ref> <ref>PMID:15539472</ref> <ref>PMID:15964670</ref> <ref>PMID:17259259</ref> <ref>PMID:17369371</ref> <ref>PMID:18248592</ref> <ref>PMID:18273012</ref> <ref>PMID:18378893</ref> <ref>PMID:19251906</ref> <ref>PMID:19484493</ref> <ref>PMID:23263767</ref> <ref>PMID:25010425</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cell fate in eukaryotes is controlled by mitogen-activated protein kinases (MAPKs) that translate external cues into cellular responses. In plants, two MAPKs-MPK3 and MPK6-regulate diverse processes of development, environmental response and immunity. However, the mechanism that bridges these shared signalling components with a specific target remains unresolved. Focusing on the development of stomata-epidermal valves that are essential for gas exchange and transpiration-here, we report that the basic helix-loop-helix protein SCREAM functions as a scaffold that recruits MPK3/6 to downregulate SPEECHLESS, a transcription factor that initiates stomatal cell lineages. SCREAM directly binds to MPK3/6 through an evolutionarily conserved, yet unconventional, bipartite motif. Mutations in this motif abrogate association, phosphorylation and degradation of SCREAM, unmask hidden non-redundancies between MPK3 and MPK6, and result in uncontrolled stomatal differentiation. Structural analyses of MPK6 with a resolution of 2.75 A showed bipartite binding of SCREAM to MPK6 that is distinct from an upstream MAPKK. Our findings elucidate, at the atomic resolution, the mechanism that directly links extrinsic signals to transcriptional reprogramming during the establishment of stomatal cell fate, and highlight a unique substrate-binding mode adopted by plant MAPKs. | ||
| + | |||
| + | Bipartite anchoring of SCREAM enforces stomatal initiation by coupling MAP kinases to SPEECHLESS.,Putarjunan A, Ruble J, Srivastava A, Zhao C, Rychel AL, Hofstetter AK, Tang X, Zhu JK, Tama F, Zheng N, Torii KU Nat Plants. 2019 Jul;5(7):742-754. doi: 10.1038/s41477-019-0440-x. Epub 2019 Jun , 24. PMID:31235876<ref>PMID:31235876</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6dtl" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 06:17, 10 July 2019
Mitogen-activated protein kinase 6
| |||||||||||
