Regulatory Functions of Nuclear Hexokinase1 Complex in Glucose Signaling

Young Hee Cho; Sang Dong Yoo; Jen Sheen

doi:10.1016/j.cell.2006.09.028

Regulatory Functions of Nuclear Hexokinase1 Complex in Glucose Signaling

Young Hee Cho, Sang Dong Yoo, Jen Sheen

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328 Citations (Scopus)

Abstract

Arabidopsis hexokinase1 (HXK1) is a glucose sensor that integrates nutrient and hormone signals to govern gene expression and plant growth in response to environmental cues. How the metabolic enzyme mediates glucose signaling remains a mystery. By coupling proteomic and binary-interaction screens, we discover two nuclear-specific HXK1 unconventional partners: the vacuolar H⁺-ATPase B1 (VHA-B1) and the 19S regulatory particle of proteasome subunit (RPT5B). Remarkably, vha-B1 and rpt5b mutants uniquely share a broad spectrum of glucose response defects with the HXK1 mutant gin2 (glucose-insensitive2). Genetic and chromatin immunoprecipitation analyses suggest that the nuclear HXK1 forms a glucose signaling complex core with VHA-B1 and RPT5B that directly modulates specific target gene transcription independent of glucose metabolism. The findings support a model in which conserved metabolic enzymes and proteins of well-established activities may perform previously unrecognized nuclear functions.

Original language	English
Pages (from-to)	579-589
Number of pages	11
Journal	Cell
Volume	127
Issue number	3
DOIs	https://doi.org/10.1016/j.cell.2006.09.028
Publication status	Published - 2006 Nov 3

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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title = "Regulatory Functions of Nuclear Hexokinase1 Complex in Glucose Signaling",

abstract = "Arabidopsis hexokinase1 (HXK1) is a glucose sensor that integrates nutrient and hormone signals to govern gene expression and plant growth in response to environmental cues. How the metabolic enzyme mediates glucose signaling remains a mystery. By coupling proteomic and binary-interaction screens, we discover two nuclear-specific HXK1 unconventional partners: the vacuolar H+-ATPase B1 (VHA-B1) and the 19S regulatory particle of proteasome subunit (RPT5B). Remarkably, vha-B1 and rpt5b mutants uniquely share a broad spectrum of glucose response defects with the HXK1 mutant gin2 (glucose-insensitive2). Genetic and chromatin immunoprecipitation analyses suggest that the nuclear HXK1 forms a glucose signaling complex core with VHA-B1 and RPT5B that directly modulates specific target gene transcription independent of glucose metabolism. The findings support a model in which conserved metabolic enzymes and proteins of well-established activities may perform previously unrecognized nuclear functions.",

author = "Cho, {Young Hee} and Yoo, {Sang Dong} and Jen Sheen",

note = "Funding Information: We are grateful to H. Sze for generously providing VHA antibodies and stimulating discussions and Sheen Lab members for helpful comments on the manuscript. We thank the Salk Institute Genomic Analysis Laboratory for providing the sequence-indexed Arabidopsis T-DNA insertion mutants, and ABRC for providing vha-C seeds. This work was supported by grants from the NSF (IOB-0217191 and DBI-0077692) and NIH (R01 GM060493) to J.S. ",

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doi = "10.1016/j.cell.2006.09.028",

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PY - 2006/11/3

Y1 - 2006/11/3

N2 - Arabidopsis hexokinase1 (HXK1) is a glucose sensor that integrates nutrient and hormone signals to govern gene expression and plant growth in response to environmental cues. How the metabolic enzyme mediates glucose signaling remains a mystery. By coupling proteomic and binary-interaction screens, we discover two nuclear-specific HXK1 unconventional partners: the vacuolar H+-ATPase B1 (VHA-B1) and the 19S regulatory particle of proteasome subunit (RPT5B). Remarkably, vha-B1 and rpt5b mutants uniquely share a broad spectrum of glucose response defects with the HXK1 mutant gin2 (glucose-insensitive2). Genetic and chromatin immunoprecipitation analyses suggest that the nuclear HXK1 forms a glucose signaling complex core with VHA-B1 and RPT5B that directly modulates specific target gene transcription independent of glucose metabolism. The findings support a model in which conserved metabolic enzymes and proteins of well-established activities may perform previously unrecognized nuclear functions.

AB - Arabidopsis hexokinase1 (HXK1) is a glucose sensor that integrates nutrient and hormone signals to govern gene expression and plant growth in response to environmental cues. How the metabolic enzyme mediates glucose signaling remains a mystery. By coupling proteomic and binary-interaction screens, we discover two nuclear-specific HXK1 unconventional partners: the vacuolar H+-ATPase B1 (VHA-B1) and the 19S regulatory particle of proteasome subunit (RPT5B). Remarkably, vha-B1 and rpt5b mutants uniquely share a broad spectrum of glucose response defects with the HXK1 mutant gin2 (glucose-insensitive2). Genetic and chromatin immunoprecipitation analyses suggest that the nuclear HXK1 forms a glucose signaling complex core with VHA-B1 and RPT5B that directly modulates specific target gene transcription independent of glucose metabolism. The findings support a model in which conserved metabolic enzymes and proteins of well-established activities may perform previously unrecognized nuclear functions.

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JO - Cell

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Regulatory Functions of Nuclear Hexokinase1 Complex in Glucose Signaling

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