In Vitro Binding of Plasma Membrane-coated Vesicle Adaptors to the Cytoplasmic Domain of Lysosomal Acid Phosphatase*

SOSA MA; SCHMIDT B; VON FIGURA K; HILLE-REHFEL A

JOURNAL OF BIOLOGICAL CHEMISTRY

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

Año: 1993 vol. 268 p. 12537 - 12543

0021-9258

Sorting of the newly synthesized membrane-boundprecursor of lysosomal acid phosphatase (LAP) involvesinternalization from the plasma membrane viaclathrin-coated pits. Using an in vitro systemw, e presentdirect evidence for high affinity interaction of thecytoplasmic domain of LAP with the amino-terminaltrunk portion of plasma membrane-coated vesicleadaptors. Coated vesicle adaptors of the trans-Golginetwork displayed poor binding to LAP, but high affinitybinding to the cytoplasmic tail of the 46-kDamannose 6-phosphate receptor, which is included inclathrin-coated pits of the trans-Golgi network. Bindingof plasma membrane adaptors to the tail peptide ofLAP required an internalization signal that containseither tyrosine or phenylalanine.