A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3

Autor: Stefan Höning, I. V. Sandoval, K von Figura
Rok vydání: 1998
Předmět:
CD36 Antigens
Cytoplasm
Swine
Acid Phosphatase
Molecular Sequence Data
Coated vesicle
Nerve Tissue Proteins
Biosensing Techniques
Monomeric Clathrin Assembly Proteins
Clathrin
General Biochemistry
Genetics and Molecular Biology
03 medical and health sciences
Cytosol
0302 clinical medicine
Antigens
CD
Leucine
Animals
Lysosome-associated membrane glycoprotein
Amino Acid Sequence
Molecular Biology
Integral membrane protein
030304 developmental biology
0303 health sciences
Membrane Glycoproteins
General Immunology and Microbiology
biology
Monophenol Monooxygenase
General Neuroscience
Brain
Lysosome-Associated Membrane Glycoproteins
Signal transducing adaptor protein
Phosphoproteins
Cell biology
Vesicular transport protein
Adaptor Proteins
Vesicular Transport
biology.protein
Melanocytes
Clathrin adaptor proteins
Lysosomes
Peptides
030217 neurology & neurosurgery
Research Article
Protein Binding
Zdroj: The EMBO Journal. 17:1304-1314
ISSN: 1460-2075
DOI: 10.1093/emboj/17.5.1304
Popis: Among the various coats involved in vesicular transport, the clathrin associated coats that contain the adaptor complexes AP-1 and AP-2 are the most extensively characterized. The function of the recently described adaptor complex AP-3, which is similar to AP-1 and AP-2 in protein composition but does not associate with clathrin, is not known. By monitoring surface plasmon resonance we observed that AP-3 is able to interact with the tail of the lysosomal integral membrane protein LIMP-II and that this binding depends on a DEXXXLI sequence in the LIMP-II tail. Furthermore, AP-3 bound to the cytoplasmic tail of the melanosome-associated protein tyrosinase which contains a related EEXXXLL sequence. The tails of LIMP-II and tyrosinase either did not interact, or only interacted poorly, with AP-1 or AP-2. In contrast, the cytoplasmic tails of other membrane proteins containing di-leucine and/or tyrosine-based sorting signals did not bind AP-3, but AP-1 and/or AP-2. This points to a function of AP-3 in intracellular sorting to lysosomes and melanosomes of a subset of cargo proteins via di-leucine-based sorting motifs.
Databáze: OpenAIRE
Externí odkaz: