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Lipid transfer protein CaMBP10 binds to glyceraldehyde-3-phosphate dehydrogenase and modulates its activity

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Abstract

Lipid transfer proteins (LTPs) are a protein family found in plants with a variety of functions. In addition to lipid binding, LTPs also bind to calmodulin and Ca2+-dependent protein kinase (CDPK), which are calcium signal transducers. For the first time, we identified glyceraldehyde-3- phosphate dehydrogenase (GAPDH) as a novel binding protein of LTP-CaMBP10 in Chinese cabbage. This binding was confirmed using multiple biochemical approaches. The effects of this interaction on GAPDH activity were assessed for both recombinant and endogenous GAPDH proteins. LTP-CaMBP10 does not appear to affect nicotinamide adenine dinucleotide (NAD)-dependent GAPDH activity. In contrast, it significantly suppresses nicotinamide adenine dinucleotide phosphate (NADPH) consumption by GAPDH in a dosage-dependent manner. This result indicated a specific role of GAPDH in regulating LTP functions and implicating crosstalk between LTP-dependent and GAPDH-dependent biological events.

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Abbreviations

LTP:

Lipid transfer proteins

CaMBP10:

Calmodulin-binding protein-10

CDPK:

Ca2+-dependent protein kinase

GAPDH:

Glyceraldehyde-3-phosphate dehydrogenase

NAD:

Nicotinamide adenine dinucleotide

NADPH:

Nicotinamide adenine dinucleotide phosphate

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Acknowledgments

This work was supported by the National Natural Science Foundation of China (No. 30871614) and Tianjin Natural Science Foundation (No. 08JCYBJC04100). Thanks to Zhe Wang from University of British Columbia for valuable discussions regarding this work and proofreading this manuscript.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, Nankai University, Tianjin, 300071, China

    Tieliang Pang, Jing Zhao & Cuifeng Li

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  1. Tieliang Pang
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  2. Jing Zhao
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  3. Cuifeng Li
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Correspondence to Cuifeng Li.

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Pang, T., Zhao, J. & Li, C. Lipid transfer protein CaMBP10 binds to glyceraldehyde-3-phosphate dehydrogenase and modulates its activity. J. Plant Biochem. Biotechnol. 25, 294–300 (2016). https://doi.org/10.1007/s13562-015-0341-7

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