The significance of post-translational modification of proteins by phosphorylation in the regulation of plant development and metabolism

Fallon, Kevin M.; Trewavas, A.J.

doi:10.1017/cbo9780511600401.005

Cited by 5 publications

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“…Light signalling mechanisms in plants are usually modulated by various post-translational modifications such as phosphorylation/dephosphorylation [14]. Phytochromes can function as serine/threonine kinases due to the conserved HKRD in their C-terminal regions [15,16] and can phosphorylate a number of phytochrome-interacting proteins including PKS1 [11], Aux/IAA [17] and the cryptochromes 1 and 2 [18].…”

Section: Introductionmentioning

confidence: 99%

A novel protein phosphatase indirectly regulates phytochrome-interacting factor 3 via phytochrome

Phee

Kim

Shin

et al. 2008

Biochemical Journal

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Light signal transduction in plants involves an intricate series of pathways which is finely regulated by interactions between specific signalling proteins, as well as by protein modifications such as phosphorylation and ubiquitination. The identification of novel phytochrome-interacting proteins and the precise signalling mechanisms that they mediate is still ongoing. In our present study, we show that the newly identified putative phytochrome-associated protein, PAPP2C (phytochrome-associated protein phosphatase type 2C), interacts in the nucleus with phyA (phytochrome A) and phyB, both in vitro and in vivo. Moreover, the phosphatase activity of PAPP2C and its association with phytochromes were found to be enhanced by red light, indicating that it plays a role in mediating phytochrome signalling. In particular, PAPP2C specifically binds to the N-terminal PHY domain of the phytochromes. We thus speculate that this interaction reflects a unique regulatory function of this phosphatase toward established phytochrome-associated proteins. We also show that PAPP2C effectively dephosphorylates phytochromes in vitro. Interestingly, PAPP2C indirectly mediates the dephosphorylation of PIF3 (phytochrome-interacting factor 3) in vitro. Taken together, we suggest that PAPP2C functions as a regulator of PIF3 by dephosphorylating phytochromes in the nucleus.

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Section: Introductionmentioning

confidence: 99%

A novel protein phosphatase indirectly regulates phytochrome-interacting factor 3 via phytochrome

Phee

Kim

Shin

et al. 2008

Biochemical Journal

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“…Although protein kinases and phosphatases are present throughout the whole plant cell, the role of the majority of them is as yet unclear and stimulus/response coupling starts to emerge in only a few cases (for review, see Fallon and Trewavas 1993;Huber et al 1994). One of the suggested functions of protein phosphorylation is in cellular memory.…”

Section: Discussionmentioning

confidence: 99%

“…Like G-proteins, protein kinases and phosphatases are not only important elements of visual transduction chains in vertebrates and invertebrates (Fowles and Akhtar 1989;Rayer et al 1990), but are also involved in red and blue light responses in higher plants and general light regulation of plant enzyme activities (Warpeha et al 1991;Shimazaki et al 1992;Fallon and Trewavas 1993;Hager et al 1993;MacKintosh and MacKintosh 1993;Terryn et al 1993). To our knowledge, no detailed analysis of reversible protein phosphorylation has yet been published for preparations of eyespot apparatuses from green algae.…”

Section: Introductionmentioning

confidence: 99%

Calcium modulates rapid protein phosphorylation/dephosphorylation in isolated eyespot apparatuses of the green alga Spermatozopsis similis

Lindén

Kreimer

1995

Planta

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Abstract.We present an initial characterization of protein kinase and phosphatase activities associated with isolated eyespot apparatuses, the organelle involved in blue/ green-light-mediated behavioural responses of flagellate green algae. In the presence of the phosphatase inhibitors okadaic acid and vanadate, rapid overall protein phosphorylation (to.5 ~ 10 s) was observed. The majority of protein kinase activities and their substrates were identified as integral or tightly-bound peripheral membrane proteins. While vanadate generally increased the phosphate incorporation into all phosphoproteins, okadaic acid specifically enhanced phosphorylation of proteins in the range of 39~13 kDa. In contrast to all other phosphoproteins in this subcellular fraction, two proteins with apparent molecular masses of 83 and 16 kDa shared remarkable similarities: (i) They exhibited a fast turnover of the 32p-label, even in the presence of phosphatase inhibitors, and (ii) their dephosphorylation was delayed at 10 -8 M free Ca 2+. In addition, the 16-kDa protein underwent thiophosphorylation. The general in-vitro phosphorylation pattern was strongly influenced by alterations of free Ca 2+ in a concentration range known to affect responses related to phototactic and photophobic behaviour of this alga (10-8 M to 10-7 M). However, characteristics of Ca 2 +-calmodulin-dependent protein kinases were not observed, i.e. exogenous calmodulin and trifluoperazine had no significant effect on protein phosphorylation. Also exogenous lipids (phosphatidylserine, diacylglycerol), inhibitors of cGMP-and cAMP-dependent protein kinases and protein kinase C (H-7 and HA-1004) as well as exogenously added cGMP and cAMP did not potentiate or inhibit protein phosphorylation. These characteristics of the kinase activity in our fraction most closely resemble those of the plant-and protist-specific group of Ca 2 +-dependent, calmodulin-independent protein kinases. In-situ phosphorylation experiments following electrophoretic separation revealed the presence of three putative Ca 2 +-dependent kinases or their catalytic subunits (77,48 and 47 kDa) in the eyespot preparation.Correspondence to: G. Kreimer; FAX: 49 (221) 470 5181 In addition, a Ca 2 +-independent activity at 28 kDa was detected. Possible roles of reversible protein phosphorylation in eyespot apparatuses are discussed.

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“…One promising area of proteomic research is using 2D gels to follow these post-translational modifications in order to discover how regulation or signal transduction might be occurring through these modifications. Some plastid enzymes, such as the Dl protein of Photosystem II, chlorophyll alb binding protein, Rubisco, PEP carboxylase, and sucrose phosphate synthase, are regulated through post-translational modifications (Fallon and Trewavas, 1993;. The results from this thesis suggest that many other maize plastid proteins are also modified.…”

Section: Discussionmentioning

confidence: 86%

Proteomics of the developing chloroplast in maize

Lonosky¹

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I would like to thank firstly, my committee for ideas, suggestions, and constructive criticism on this research. I would also like to thank Aigen Fu for teaching me proteomic techniques and his help in solving technical problems, Xiaosi Zhang for performing the statistics on the data and for answering my numerous questions, and Andrea Flack for problem solving, writing advice, and overall general support. I am grateful for the friendship and congeniality of the Rodermel lab members, the Spalding lab members, and the Voytas lab members. An NSF IGERT fellowship supported this research and the BCB office and Dan Voytas administrated that fellowship; thank you for your help and support. Lastly, I would like to thank my good friends, especially Ericka Havecker and Elizabeth Pettit, and my family for unfailing enthusiasm and humor, and Michael Hirsch for his encouragement.

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The significance of post-translational modification of proteins by phosphorylation in the regulation of plant development and metabolism

Cited by 5 publications

References 0 publications

A novel protein phosphatase indirectly regulates phytochrome-interacting factor 3 via phytochrome

A novel protein phosphatase indirectly regulates phytochrome-interacting factor 3 via phytochrome

Calcium modulates rapid protein phosphorylation/dephosphorylation in isolated eyespot apparatuses of the green alga Spermatozopsis similis

Proteomics of the developing chloroplast in maize

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