Handling calcium signaling: Arabidopsis CaMs and CMLs

McCormack, Elizabeth A.; Tsai, Ying-Chien; Braam, Janet

doi:10.1016/j.tplants.2005.07.001

Cited by 429 publications

(391 citation statements)

References 25 publications

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“…The 50 members of the CML gene family of A. thaliana have been proposed to encode proteins that facilitate specificity during Ca 2+ signalling (McCormack et al ., 2005; Bender & Snedden, 2013). CML41 expression was previously shown to be upregulated by flg22 (Denoux et al ., 2008), so we investigated whether it had a role in pathogen responses.…”

Section: Resultsmentioning

confidence: 99%

“…1a); therefore, it is likely that CML41 plays a similar role in PD flux regulation when challenged with soil bacterial pathogens. An investigation is also warranted into: the role of CML41 in the other tissues in which it is expressed such as senescent leaves and flowers (McCormack et al ., 2005); and, the significance of its transcriptional regulation by RNA‐dependent methylation (Baev et al ., 2010). …”

Section: Resultsmentioning

confidence: 99%

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A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses

Cheval

Laohavisit

et al. 2017

New Phytologist

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Summary Plants sense microbial signatures via activation of pattern recognition receptors (PPRs), which trigger a range of cellular defences. One response is the closure of plasmodesmata, which reduces symplastic connectivity and the capacity for direct molecular exchange between host cells.Plasmodesmal flux is regulated by a variety of environmental cues but the downstream signalling pathways are poorly defined, especially the way in which calcium regulates plasmodesmal closure.Here, we identify that closure of plasmodesmata in response to bacterial flagellin, but not fungal chitin, is mediated by a plasmodesmal‐localized Ca2+‐binding protein Calmodulin‐like 41 (CML41). CML41 is transcriptionally upregulated by flg22 and facilitates rapid callose deposition at plasmodesmata following flg22 treatment. CML41 acts independently of other defence responses triggered by flg22 perception and reduces bacterial infection.We propose that CML41 enables Ca2+‐signalling specificity during bacterial pathogen attack and is required for a complete defence response against Pseudomonas syringae.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses

Cheval

Laohavisit

et al. 2017

New Phytologist

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“…In addition to various types of CaMs, plants possess another set of proteins called the calmodulin-like (CML) proteins that have similarities to CaM but contain unique functions (14), and their compared sequence identity to CaM is lower (15). Over 50 genes identified in Arabidopsis (16) and 26 in rice encode putative CML proteins that have yet to be characterized completely. CMLs are involved in different cellular processes such as flowering of plants (where CML23 and CML24 act through the nitric oxide pathway) (17), establishment of cell polarity (CML12) (18), abiotic stress (CML9) (19,20), and DNA lesion repair (CML19) (20).…”

Section: Oscam61 Is One Of Five Calmodulins Known To Be Present Inmentioning

confidence: 99%

Structural Analysis of a Calmodulin Variant from Rice

Jamshidiha

Ishida

Sutherland

et al. 2013

Journal of Biological Chemistry

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“…However, plant genomes do not encode IQGAPs, and the mechanisms of Ca 2+ -mediated cytoskeletal organization are largely elusive (Hepler, 1992(Hepler, , 2005Wang et al, 2011). During the colonization of terrestrial habitats, novel adaptive traits evolved in land plants (Graham, 1996), and the size of plant CaM/CML families expanded greatly to provide versatility for transducing complex Ca 2+ signals into numerous cellular and environmental responses (McCormack et al, 2005;Zhu et al, 2015b). Likewise, the cytoskeleton acquired additional functions for adapting cell shape and cell growth, and a multitude of unique MAPs emerged for generating the various cytoskeletal arrays and controlling their organization and stability (Gardiner, 2013;Struk and Dhonukshe, 2014).…”

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confidence: 99%

The IQD Family of Calmodulin-Binding Proteins Links Calcium Signaling to Microtubules, Membrane Subdomains, and the Nucleus

et al. 2017

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ORCID IDs: 0000-0002-3493-4800 (K.B.); 0000-0002-7146-043X (B.M.).Calcium (Ca 2+ ) signaling and dynamic reorganization of the cytoskeleton are essential processes for the coordination and control of plant cell shape and cell growth. Calmodulin (CaM) and closely related calmodulin-like (CML) polypeptides are principal sensors of Ca 2+ signals. CaM/CMLs decode and relay information encrypted by the second messenger via differential interactions with a wide spectrum of targets to modulate their diverse biochemical activities. The plant-specific IQ67 DOMAIN (IQD) family emerged as possibly the largest class of CaM-interacting proteins with undefined molecular functions and biological roles. Here, we show that the 33 members of the IQD family in Arabidopsis (Arabidopsis thaliana) differentially localize, using green fluorescent protein (GFP)-tagged proteins, to multiple and distinct subcellular sites, including microtubule (MT) arrays, plasma membrane subdomains, and nuclear compartments. Intriguingly, the various IQD-specific localization patterns coincide with the subcellular patterns of IQD-dependent recruitment of CaM, suggesting that the diverse IQD members sequester Ca 2+ -CaM signaling modules to specific subcellular sites for precise regulation of Ca 2+ -dependent processes. Because MT localization is a hallmark of most IQD family members, we quantitatively analyzed GFP-labeled MT arrays in Nicotiana benthamiana cells transiently expressing GFP-IQD fusions and observed IQD-specific MT patterns, which point to a role of IQDs in MT organization and dynamics. Indeed, stable overexpression of select IQD proteins in Arabidopsis altered cellular MT orientation, cell shape, and organ morphology. Because IQDs share biochemical properties with scaffold proteins, we propose that IQD families provide an assortment of platform proteins for integrating CaM-dependent Ca 2+ signaling at multiple cellular sites to regulate cell function, shape, and growth.

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Handling calcium signaling: Arabidopsis CaMs and CMLs

Cited by 429 publications

References 25 publications

A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses

A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses

Structural Analysis of a Calmodulin Variant from Rice

The IQD Family of Calmodulin-Binding Proteins Links Calcium Signaling to Microtubules, Membrane Subdomains, and the Nucleus

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