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© The Rockefeller University Press, 0021-9525/2000//1335 $5.00
The Journal of Cell Biology, Volume 149, Number 7, , 2000 1335-1344

Original Article

The Plant Vacuolar Sorting Receptor Atelp Is Involved in Transport of Nh2-Terminal Propeptide-Containing Vacuolar Proteins in Arabidopsis thaliana



Sharif U. Ahmeda, Enrique Rojoa, Valentina Kovalevaa, Sridhar Venkataramana,b, James E. Dombrowskia, Ken Matsuokac, and Natasha V. Raikhela,b

a Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824
b Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824
c Laboratory of Biochemistry, Graduate School of Bio-agricultural Sciences, Nagoya University, Chikusa-ku, Nagoya 464-8601, Japan
Department of Energy, Plant Research Laboratory, Michigan State University, East Lansing, MI 48824.(517) 353-9168(517) 353-3518

nraikhel{at}pilot.msu.edu

Many soluble plant vacuolar proteins are sorted away from secreted proteins into small vesicles at the trans-Golgi network by transmembrane cargo receptors. Cleavable vacuolar sorting signals include the NH2-terminal propeptide (NTPP) present in sweet potato sporamin (Spo) and the COOH-terminal propeptide (CTPP) present in barley lectin (BL). These two proteins have been found to be transported by different mechanisms to the vacuole. We examined the ability of the vacuolar cargo receptor AtELP to interact with the sorting signals of heterologous and endogenous plant vacuolar proteins in mediating vacuolar transport in Arabidopsis thaliana. AtELP extracted from microsomes was found to interact with the NTPPs of barley aleurain and Spo, but not with the CTPPs of BL or tobacco chitinase, in a pH-dependent and sequence-specific manner. In addition, EM studies revealed the colocalization of AtELP with NTPP-Spo at the Golgi apparatus, but not with BL-CTPP in roots of transgenic Arabidopsis plants. Further, we found that AtELP interacts in a similar manner with the NTPP of the endogenous vacuolar protein AtALEU (Arabidopsis thaliana Aleu), a protein highly homologous to barley aleurain. We hypothesize that AtELP functions as a vacuolar sorting receptor involved in the targeting of NTPP-, but not CTPP-containing proteins in Arabidopsis.

Key Words: protein traffic • Golgi apparatus • COOH-terminal propeptide • plant vacuole barley aleurain

© 2000 The Rockefeller University Press

The online version of this article contains supplemental material.

Sharif U. Ahmed's current address is Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720.

James E. Dombrowski's current address is Institute of Biological Chemistry, Washington State University, Pullman, WA 99164.

Abbreviations used in this paper: AtALEU, Arabidopsis thaliana Aleu; barley Aleu, barley aleurain; BL, barley lectin; CCVs, clathrin-coated vesicles; CTPP, COOH-terminal propeptide; LV, lytic vacuole; Mt, mutant; NTPP, NH2-terminal propeptide; ORF, open reading frame; PI, phosphatidylinositol; PVC, prevacuolar compartment; Spo, sporamin; TGN, trans-Golgi network; TobChit, tobacco chitinase; Wt, wild-type.


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