Subcellular localization and membrane topology of the melon ethylene receptor CmERS1.

Abstract:

:Ethylene receptors are multispanning membrane proteins that negatively regulate ethylene responses via the formation of a signaling complex with downstream elements. To better understand their biochemical functions, we investigated the membrane topology and subcellular localization of CmERS1, a melon (Cucumis melo) ethylene receptor that has three putative transmembrane domains at the N terminus. Analyses using membrane fractionation and green fluorescent protein imaging approaches indicate that CmERS1 is predominantly associated with the endoplasmic reticulum (ER) membrane. Detergent treatments of melon microsomes showed that the receptor protein is integrally bound to the ER membrane. A protease protection assay and N-glycosylation analysis were used to determine membrane topology. The results indicate that CmERS1 spans the membrane three times, with its N terminus facing the luminal space and the large C-terminal portion lying on the cytosolic side of the ER membrane. This orientation provides a platform for interaction with the cytosolic signaling elements. The three N-terminal transmembrane segments were found to function as topogenic sequences to determine the final topology. High conservation of these topogenic sequences in all ethylene receptor homologs identified thus far suggests that these proteins may share the same membrane topology.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Ma B,Cui ML,Sun HJ,Takada K,Mori H,Kamada H,Ezura H

doi

10.1104/pp.106.080523

subject

Has Abstract

pub_date

2006-06-01 00:00:00

pages

587-97

issue

2

eissn

0032-0889

issn

1532-2548

pii

pp.106.080523

journal_volume

141

pub_type

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