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Plant Physiology 98:264-272 (1992)
© 1992 American Society of Plant Biologists

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Cellular and Structural Biology

Arabinogalactan-Rich Glycoproteins Are Localized on the Cell Surface and in Intravacuolar Multivesicular Bodies 1,2

Eliot M. Herman and Christopher J. Lamb

Plant Molecular Biology Laboratory, United States Department of Agriculture, Agricultural Research Service, Beltsville, Maryland 20705, Plant Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037

We investigated the subcellular distribution of antigenic sites immunoreactive to the monoclonal antibody 16.4B4 (PM Norman, VPM Wingate, MS Fitter, CJ Lamb [1986] Planta 167: 452-459) in tobacco (Nicotiana tabacum) leaf cells. This antibody is directed against a glycan epitope in a family of plasma membrane arabinogalactan proteins of 135 to 180 kilodaltons, elaborated from a polypeptide of relative molecular mass 50 kilodaltons (PM Norman, P Kjellbom, DJ Bradley, MG Hahn, CJ Lamb [1990] Planta 181: 365-373). We demonstrated by immunogold electron microscopy that the epitope reactive with monoclonal antibody 16.4B4 is localized on the cell surface in the leaf parenchyma cell periplast. The 16.4B4 antigen is also localized in multivesicular invaginations of the plasma membrane also known as plasmalemmasomes, implying a biochemical and, hence, functional interrelationship between these structures. Monoclonal antibody 16.4B4 also labels intracellular multivesicular bodies that appear to represent internalized plasmalemmasomes. Antibody reactivity was also observed in partially degraded multivesicular bodies sequestered within the central vacuole. We propose that the subcellular distribution of the epitope reactive with monoclonal antibody 16.4B4 defines a plasmalemmasome (or multivesicular body-mediated) pathway for the internalization of the periplasmic matrix for vacuolar mediated disposal. The multivesicular bodies appear to be equivalent to the well-characterized endosomes and multivesicular bodies of animal cells involved in the internalization and lysosome-mediated degradation of extracellular materials.

1 Research in the laboratory of E.M.H. is supported by the U.S. Department of Agriculture Office of Competitive Grants. Research in the laboratory of C.J.L. was supported by the McKnight Foundation, the U.S. Department of Agriculture Office of Competitive Grants (83-CRCR-1-1251), and the Samuel Roberts Noble Foundation.

2 This paper is dedicated to the memory of ASPP member Dr. Leland (Lee) M. Shannon (1927-1991), Professor of Biochemistry and Dean of the Graduate Division at the University of California, Riverside. Lee was widely known for his laboratory's research on the legume seed lectins. Lee will be greatly missed by his friends and colleagues.




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