Conservation of the Cold Shock Domain Protein Family in Plants

Karlson, Dale; Imai, Ryozo

doi:10.1104/pp.014472

Cited by 127 publications

(130 citation statements)

References 16 publications

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“…Both changes (rigidification and fluidization) are perceived as primary stimuli signals that trigger fluxes of second messengers (e.g., Ca ?2 ) to activate specific heat response. Heat responses include the production and activation of heat shock proteins (HSPs) (Vierling 1991); heat shock transcription factors (HSFs); cold shock domain containing proteins (CSDPs) (Karlson and Imai 2003); ROS scavengers; antioxidants; compatible solutes; calcium-dependent protein kinases (CDPKs) and MAP kinases.…”

Section: Mapks and Temperature Stressesmentioning

confidence: 99%

MAPK cascades and major abiotic stresses

et al. 2014

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Plants have evolved with complex signaling circuits that operate under multiple conditions and govern numerous cellular functions. Stress signaling in plant cells is a sophisticated network composed of interacting proteins organized into tiered cascades where the function of a molecule is dependent on the interaction and the activation of another. In a linear scheme, the receptors of cell surface sense the stimuli and convey stress signals through specific pathways and downstream phosphorylation events controlled by mitogen-activated protein (MAP) kinases and second messengers, leading to appropriate adaptive responses. The specificity of the pathway is guided by scaffolding proteins and docking domains inside the interacting partners with distinctive structures and functions. The flexibility and the fine-tuned organization of the signaling molecules drive the activated MAP kinases into the appropriate location and connection to control and integrate the information flow. Here, we overview recent findings of the involvement of MAP kinases in major abiotic stresses (drought, cold and temperature fluctuations) and we shed light on the complexity and the specificity of MAP kinase signaling modules.

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Section: Mapks and Temperature Stressesmentioning

confidence: 99%

MAPK cascades and major abiotic stresses

et al. 2014

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“…The expression of CspA and CspB in transgenic rice improved the growth of plants under the effect of a number of abiotic factors like cold, heat and water deficit. The expression of bacterial CSPs increased cold tolerance in transgenic Arabidopsis (Karlson & Imai 2003;Nakaminami et al 2006;Castiglioni et al 2008). Some PR (pathogenrelated) proteins such as PR1, PR2, PR5, PR10, PR11 and PR14 are approved to be up-regulated by low-temperature treatment (Seo et al 2008;Zhang et al 2010).…”

Section: Gene Expression Induction In Response To Low Temperaturementioning

confidence: 99%

Advances in physiological and molecular aspects of plant cold tolerance

Rihan

Al-Issawi

Fuller

2017

Journal of Plant Interactions

105

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“…WCSP1 complements the cold sensitive phenotype of the quadruple Csp-deletion strain of E. coli (BX04), indicating that this protein can function as an RNA chaperone in vivo in a bacterial system (30). Expression studies revealed that some Arabidopsis CSP transcripts are also increased upon cold stress treatment, indicating a potential role in cold adaptation (19,31,32). Arabidopsis thaliana cold shock domain proteins (AtCSPs) promote cold adaptation in bacteria (31)(32)(33)(34).…”

Section: Functions In Cold Stress Adaptationmentioning

confidence: 99%

“…Higher plant CSPs are glycine-rich proteins and are distinct in that they contain two types of nucleic acid-binding modules, a single N-terminal CSD and variable numbers of C-terminal retroviral-like CCHC zinc fingers that are interspersed by glycine-rich regions (see Fig. 1) (19).…”

Section: Structure Of Cold Shock Domain Proteinsmentioning

confidence: 99%

Conservation of the Cold Shock Domain Protein Family in Plants

Cited by 127 publications

References 16 publications

MAPK cascades and major abiotic stresses

MAPK cascades and major abiotic stresses

Advances in physiological and molecular aspects of plant cold tolerance

Comparison of structure, function and regulation of plant cold shock domain proteins to bacterial and animal cold shock domain proteins

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