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J. Cell Biol.,
Volume 139, Number 4, November 17, 1997 929-940
* Dyson Vision Research Institute, Department of Ophthalmology, and Department of Cell Biology, Cornell University Medical
College, New York 10021; Delivery of newly synthesized membrane-spanning proteins to the apical plasma membrane domain of polarized MDCK epithelial cells is dependent
on yet unidentified sorting signals present in the luminal domains of these proteins. In this report we show that structural information for apical sorting of transmembrane neurotrophin receptors (p75NTR) is localized
to a juxtamembrane region of the extracellular domain
that is rich in O-glycosylated serine/threonine residues. An internal deletion of 50 amino acids that removes
this stalk domain from p75NTR causes the protein to be
sorted exclusively of the basolateral plasma membrane.
Basolateral sorting stalk-minus p75NTR does not occur
by default, but requires sequences present in the cytoplasmic domain. The stalk domain is also required for apical secretion of a soluble form of p75NTR, providing
the first demonstration that the same domain can mediate apical sorting of both a membrane-anchored as well
as secreted protein. However, the single N-glycan
present on p75NTR is not required for apical sorting of
either transmembrane or secreted forms.
Department of Neurobiology, Stanford University School of Medicine, Stanford, California 94305;
and § Laboratoire de Genetique et Physiologie du Developpement, Unite Mixte de Recherche 9943 Faculte des Sciences de
Luminy, 13288 Marseille, Cedex 09 France
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