PMID: 8580760Jan 1, 1995Paper

Regulation of synthesis and turnover of maize auxin-binding protein and observations on its passage to the plasma membrane: comparisons to maize immunoglobulin-binding protein cognate

Planta
S C OliverR M Napier

Abstract

Electrophysiological experiments have indicated that a fraction of the major auxin-binding protein (ABP1) of maize (Zea mays L.) might be a receptor on the outer surface of the plasma membrane. The predominant location of ABP1 is in the lumen of the endoplasmic reticulum (ER), in accord with its C-terminal KDEL retention signal. Little is known about the biology of the protein in vivo or the rate at which it might pass to the cell surface. We have examined the turnover of ABP1 by in vivo labelling of maize coleoptile sections. After different chase times, ABP1 was immunoprecipitated from detergent-solubilised membrane preparations. Two polypeptides coprecipitated with ABP1. Neither was recognised by any ABP1 antibodies nor by monoclonals to ER retention sequences. The possible significance of these coprecipitating polypeptides is discussed. In addition, we have used a monoclonal antibody to precipitate HDEL proteins from the same membrane preparations. Two dimensional electrophoresis and N-terminal sequencing showed that the major HDEL protein precipitated was a member of the heat-shock-protein 70 family, a homologue of BiP (immunoglobulin-binding protein). We have investigated the turnover of this BiP homologue for comparison ...Continue Reading

Citations

Oct 3, 2009·Plant Cell Reports·Kishore C S PanigrahiMan Mohan Johri
Jun 28, 2005·The FEBS Journal·Shinya KamauchiReiko Urade
Jan 25, 2012·The Plant Journal : for Cell and Molecular Biology·Zhen WangChristoph Benning
Jun 7, 2015·Journal of Experimental Botany·Jisheng ChenZhenbiao Yang

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