Cloning of a cdc2-related protein kinase from Trypanosoma cruzi that interacts with mammalian cyclins1Note: The nucleotide sequences reported in this paper has been submitted to the GenBankTM/EMBL data bank with accession numbers tzcrk3, U69958; tzcrk3a, U69960; tzcrk3b U69959; tzcrk1, U74762; tzcrk1a, U74763; tzcrk1b, U74764; tzcrk1c, U74765; tzcrk1d, U74766.1

Reversible phosphorylation is a major mechanism for regulating protein function and controls a wide range of cellular functions including responses to external stimuli. The plant-specific SNF1-related protein kinase 2s (SnRK2s) function as central regulators of plant growth and development, as well as tolerance to multiple abiotic stresses. Although the activity of SnRK2s is tightly regulated in a phytohormone abscisic acid (ABA)-dependent manner, recent investigations have revealed that SnRK2s can be activated by group B Raf-like protein kinases independently of ABA. Furthermore, evidence is accumulating that SnRK2s modulate plant growth through regulation of target of rapamycin (TOR) signaling. Here, we summarize recent advances in knowledge of how SnRK2s mediate plant growth and osmotic stress signaling and discuss future challenges in this research field.

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Identification of a Ras-related protein in murine erythroleukemia cells that is a cAMP-dependent protein kinase substrate and is phosphorylated during chemically induced differentiation.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)80661-0 ◽

2000 ◽

Vol 275 (19) ◽

pp. 14777

Author(s):

Jurgen S. Scheele ◽

Renate B. Pilz ◽

Lawrence A. Quilliam ◽

Gerry R. Boss

Keyword(s):

Protein Kinase ◽

Related Protein ◽

Induced Differentiation ◽

Dependent Protein Kinase ◽

Kinase Substrate ◽

Erythroleukemia Cells ◽

Chemically Induced ◽

Dependent Protein ◽

Murine Erythroleukemia ◽

Murine Erythroleukemia Cells

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Phosphorylation of tau protein by purified p34cdc28 and a related protein kinase from neurofilaments.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)41832-7 ◽

1992 ◽

Vol 267 (27) ◽

pp. 19705-19709 ◽

Cited By ~ 4

Author(s):

M Mawal-Dewan ◽

P.C. Sen ◽

M Abdel-Ghany ◽

D Shalloway ◽

E Racker

Keyword(s):

Protein Kinase ◽

Tau Protein ◽

Related Protein

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Mechanism of Activation of NDR (Nuclear Dbf2-related) Protein Kinase by the hMOB1 Protein

Journal of Biological Chemistry ◽

10.1074/jbc.m404542200 ◽

2004 ◽

Vol 279 (34) ◽

pp. 35228-35235 ◽

Cited By ~ 98

Author(s):

Samuel J. Bichsel ◽

Rastislav Tamaskovic ◽

Mario R. Stegert ◽

Brian A. Hemmings

Keyword(s):

Protein Kinase ◽

Related Protein

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SNF1-related protein kinase 1: the many-faced signaling hub regulating developmental plasticity in plants

Journal of Experimental Botany ◽

10.1093/jxb/erab079 ◽

2021 ◽

Author(s):

Muhammed Jamsheer K ◽

Manoj Kumar ◽

Vibha Srivastava

Keyword(s):

Protein Kinase ◽

Environmental Conditions ◽

Protein Trafficking ◽

Developmental Plasticity ◽

Inositol Phosphate ◽

Future Research ◽

Primary Metabolism ◽

Related Protein ◽

Comprehensive Overview ◽

Cellular Processes

AbstractThe Snf1-related protein kinase 1 (SnRK1) is the plant homolog of the heterotrimeric AMP-activated protein kinase/sucrose non-fermenting 1 (AMPK/Snf1), which works as a major regulator of growth under nutrient-limiting conditions in eukaryotes. Along with its conserved role as a master regulator of sugar starvation responses, SnRK1 is involved in controlling the developmental plasticity and resilience under diverse environmental conditions in plants. In this review, through mining and analyzing the interactome and phosphoproteome data of SnRK1, we are highlighting its role in fundamental cellular processes such as gene regulation, protein synthesis, primary metabolism, protein trafficking, nutrient homeostasis, and autophagy. Along with the well-characterized molecular interaction in SnRK1 signaling, our analysis highlights several unchartered regions of SnRK1 signaling in plants such as its possible communication with chromatin remodelers, histone modifiers, and inositol phosphate signaling. We also discuss potential reciprocal interactions of SnRK1 signaling with other signaling pathways and cellular processes, which could be involved in maintaining flexibility and homeostasis under different environmental conditions. Overall, this review provides a comprehensive overview of the SnRK1 signaling network in plants and suggests many novel directions for future research.

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