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PLANT PHYSIOLOGY , Vol 101, Issue 2 595-606, Copyright © 1993 by American Society of Plant Biologists
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DEVELOPMENT AND GROWTH REGULATION |
KDEL-Containing Auxin-Binding Protein Is Secreted to the Plasma Membrane and Cell Wall
A. M. Jones and E. M. Herman
Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599 (A.M.J.)
The auxin-binding protein ABP1 has been postulated to mediate auxin-induced
cellular changes associated with cell expansion. This protein contains the
endoplasmic reticulum (ER) retention signal, the tetrapeptide
lysine-aspartic acid-glutamic acid-leucine (KDEL), at its carboxy terminus,
consistent with previous subcellular fractionation data that indicated an
ER location for ABP1. We used electron microscopic immunocytochemistry to
identify the subcellular localization of ABP1. Using maize (Zea mays)
coleoptile tissue and a black Mexican sweet (BMS) maize cell line, we found
that ABP1 is located in the ER as expected, but is also on or closely
associated with the plasma membrane and within the cell wall. Labeling of
the Golgi apparatus suggests that the transport of ABP1 to the cell wall
occurs via the secretory system. Inhibition of secretion of an ABP homolog
into the medium of BMS cell cultures by brefeldin A, a drug that
specifically blocks secretion, is consistent with this secretion pathway.
The secreted protein was recognized by an anti-KDEL peptide antibody,
strongly supporting the interpretation that movement of this protein out of
the ER does not involve loss of the carboxy-terminal signal. Cells starved
for 2,4-dichlorophenoxyacetic acid for 72 h retained less ABP in the cell
and secreted more of it into the medium. The significance of our
observations is 2-fold. We have identified a KDEL-containing protein that
specifically escapes the ER retention system, and we provide an explanation
for the apparent discrepancy that most of the ABP is located in the ER,
whereas ABP and auxin act at the plasma membrane.
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