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Cited by 391

The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.

Protein Phosphorylation in Amyloplasts Regulates Starch Branching Enzyme Activity and Protein–Protein Interactions

Open access
Tetlow, Ian J., Wait, Robin, Lu, Zhenxiao, Akkasaeng, Rut, Bowsher, Caroline G., Esposito, Sergio, Kosar-Hashemi, Behjat, Morell, Matthew K., Emes, Michael J.·2004·The Plant Cell
DOI 10.1105/tpc.017400
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Abstract

Protein phosphorylation in amyloplasts and chloroplasts of Triticum aestivum (wheat) was investigated after the incubation of intact plastids with gamma-(32)P-ATP. Among the soluble phosphoproteins detected in plastids, three forms of starch branching enzyme (SBE) were phosphorylated in amyloplasts (SBEI, SBEIIa, and SBEIIb), and both forms of SBE in chloroplasts (SBEI and SBEIIa) were shown to be phosphorylated after sequencing of the immunoprecipitated (32)P-labeled phosphoproteins using quadrupole-orthogonal acceleration time of flight mass spectrometry. Phosphoamino acid analysis of the phosphorylated SBE forms indicated that the proteins are all phosphorylated on Ser residues. Analysis of starch granule-associated phosphoproteins after incubation of intact amyloplasts with gamma-(32)P-ATP indicated that the granule-associated forms of SBEII and two granule-associated forms of starch synthase (SS) are phosphorylated, including SSIIa. Measurement of SBE activity in amyloplasts and chloroplasts showed that phosphorylation activated SBEIIa (and SBEIIb in amyloplasts), whereas dephosphorylation using alkaline phosphatase reduced the catalytic activity of both enzymes. Phosphorylation and dephosphorylation had no effect on the measurable activity of SBEI in amyloplasts and chloroplasts, and the activities of both granule-bound forms of SBEII in amyloplasts were unaffected by dephosphorylation. Immunoprecipitation experiments using peptide-specific anti-SBE antibodies showed that SBEIIb and starch phosphorylase each coimmunoprecipitated with SBEI in a phosphorylation-dependent manner, suggesting that these enzymes may form protein complexes within the amyloplast in vivo. Conversely, dephosphorylation of immunoprecipitated protein complex led to its disassembly. This article reports direct evidence that enzymes of starch metabolism (amylopectin synthesis) are regulated by protein phosphorylation and indicate a wider role for protein phosphorylation and protein-protein interactions in the control of starch anabolism and catabolism.

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Metadata

Authors
Tetlow, I. J., Wait, R., Lu, Z., Akkasaeng, R., Bowsher, C. G., Esposito, S., Kosar-Hashemi, B., Morell, M. K., & Emes, M. J.
Venue
The Plant Cell
Publisher
Oxford University Press (OUP)
Published
2004-02-18
Volume
16
Issue
3
Pages
694-708
ISSN
  • 1040-4651 (ISSN-L)
  • 1532-298X
DOI
10.1105/tpc.017400
OpenAlex
W2037411784
Cited by
391
References
53
FWCI
5.25
Type
journal article
Language
en
Open access
bronze

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