INVESTIGADORES
SOSA ESCUDERO Miguel Angel
artículos
Título:
The 46 kDa mannose-6-phosphate receptor contains multiple binding sites for clathrin adaptors
Autor/es:
HÖNING S; SOSA MA; HILLE-REHFELD A; VON FIGURA K
Revista:
JOURNAL OF BIOLOGICAL CHEMISTRY
Editorial:
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Referencias:
Lugar: Bethesda, Maryland; Año: 1997 vol. 272 p. 19884 - 19890
ISSN:
0021-9258
Resumen:
The two known mannose 6-phosphate receptors
(MPR46 and MPR300) both mediate the transport of
Man-6-P-containing lysosomal proteins to lysosomes.
However, the MPRs cannot be detected in lysosomes,
instead they recycle between the plasma membrane and
endosomes and between endosomes and the trans-Golgi
network. Both, endocytosis from the plasma membrane
and budding of transport vesicles from the trans-Golgi
network involves the interaction of the receptor with
the clathrin-coated vesicles-associated protein complexes
AP1 and AP2. We have analyzed this interaction
between the Golgi-restricted AP1 complex and the
plasma membrane-restricted AP2 complex with the
MPR46 tail in vitro by using a biosensor.
AP1 and AP2 both bind to and dissociate from the
MPR46 tail with similar kinetics. Using synthetic peptides
corresponding to different MPR receptor tail regions
in inhibition and binding studies, a common high
affinity binding site for AP1 and AP2 and two separate
high affinity binding sites for AP1 and AP2, respectively,
were identified.