In vitro binding of plasma membrane-coated vesicle adaptors to the cytoplasmic domain of lysosomal acid phosphatase.
Sorting of the newly synthesized membrane-bound precursor of lysosomal acid phosphatase (LAP) involves internalization from the plasma membrane via clathrin-coated pits. Using an in vitro system, we present direct evidence for high affinity interaction of the cytoplasmic domain of LAP with the amino-terminal trunk portion of plasma membrane-coated vesicle adaptors. Coated vesicle adaptors of the trans-Golgi network displayed poor binding to LAP, but high affinity binding to the cytoplasmic tail of the 46-kDa mannose 6-phosphate receptor, which is included in clathrin-coated pits of the trans-Golgi network. Binding of plasma membrane adaptors to the tail peptide of LAP required an internalization signal that contains either tyrosine or phenylalanine.
Sosa
M A
MA
Universität Göttingen, Federal Republic of Germany.
Schmidt
B
B
von Figura
K
K
Hille-Rehfeld
A
A
D000135:Acid Phosphatase / Q000302:isolation & purification / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D001921:Brain / Q000201:enzymology; D002417:Cattle; D002846:Chromatography, Affinity; D003034:Coated Pits, Cell-Membrane / Q000378:metabolism*; D003600:Cytosol / Q000201:enzymology; D006056:Golgi Apparatus / Q000378:metabolism; D008247:Lysosomes / Q000201:enzymology*; D008565:Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D017527:Receptor, IGF Type 2 / Q000302:isolation & purification / Q000378:metabolism
D000911:Antibodies, Monoclonal; D008565:Membrane Proteins; D017527:Receptor, IGF Type 2; D000135:Acid Phosphatase