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United States Department of Agriculture

Agricultural Research Service

Research Project: IDENTIFYING AND MANIPULATING DETERMINANTS OF PHOTOSYNTHATE PRODUCTION AND PARTITIONING Title: Sucrose Synthase Interaction with the Voltage-Dependent Anion Channel Suggests a Potential Role for the Enzyme in Inter-Organellar Signaling

item Chalivendra, Subbaiah - UNIVERSITY OF ILLINOIS
item Huber, Steven
item Sachs, Martin
item Rhoads, David - AZ STATE UNIVERSITY

Submitted to: American Society of Plant Biologists
Publication Type: Abstract Only
Publication Acceptance Date: March 1, 2006
Publication Date: July 1, 2006
Citation: Chalivendra, S.C., Huber, S.C., Sachs, M.M., Rhoads, D.M. 2006. Sucrose synthase interaction with the voltage-dependent anion channel suggests a potential role for the enzyme in inter-organellar signaling. American Society of Plant Biologists [abstract]. Paper no. 36027. Available:

Technical Abstract: Sucrose synthase (SUS) is a key enzyme in plant sucrose catabolism and uniquely able to mobilize sucrose into multiple pathways involved in metabolic, structural, and storage functions. Our recent work indicates that the biological function of SUS extends beyond its biochemical activity. This inference is based on the following observations: a) tissue-specific, isoform-dependent and metabolically-regulated association of SUS with mitochondria and nuclei and b) isoform-specific and anoxia-enhanced interaction of SUS with the outer mitochondrial membrane protein, VDAC (voltage-dependent anion channel; also known as mitochondrial porin). Our recent work indicates that the VDAC is also localized to the nucleus in maize tissues and further, may co-localize with SUS to the same sub-nuclear compartments. We are currently analyzing the inter-compartmental dynamics of these proteins under anoxic stress and the effects of the protein cross-talk on stress-mediated gene expression, using isoform-specific antisera and mutants. Results on the role of SUS in inter-organellar signaling would be discussed. National Science Foundation is gratefully acknowledged for funding this research.

Last Modified: 4/22/2015
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