scholarly journals Localization of the signal for rapid internalization of the bovine cation-independent mannose 6-phosphate/insulin-like growth factor-II receptor to amino acids 24-29 of the cytoplasmic tail.

1991 ◽  
Vol 266 (9) ◽  
pp. 5682-5688 ◽  
Author(s):  
W M Canfield ◽  
K F Johnson ◽  
R D Ye ◽  
W Gregory ◽  
S Kornfeld
Keyword(s):  
Amino Acids ◽  
Growth Factor ◽  
Cytoplasmic Tail ◽  
Insulin Like Growth Factor ◽  
Factor Ii ◽  
Mannose 6 Phosphate

scholarly journals The cytoplasmic tail of the mannose 6-phosphate/insulin-like growth factor-II receptor has two signals for lysosomal enzyme sorting in the Golgi.

1992 ◽  
Vol 119 (2) ◽  
pp. 249-257 ◽  
Author(s):  
K F Johnson ◽  
S Kornfeld
Keyword(s):  
Plasma Membrane ◽  
Growth Factor ◽  
Cytoplasmic Tail ◽  
Adaptor Proteins ◽  
Carboxyl Terminus ◽  
Insulin Like Growth Factor ◽  
Factor Ii ◽  
Carboxyl Terminal ◽  
Mannose 6 Phosphate ◽  
Mutant Receptors

The mannose 6-phosphate/insulin-like growth factor-II (Man-6-P/IGF-II) receptor is known to cycle between the Golgi, endosomes, and the plasma membrane. In the Golgi the receptor binds newly synthesized lysosomal enzymes and transports them directly to an endosomal (prelysosomal) compartment without traversing the plasma membrane. Deletion of the carboxyl-terminal Leu-Leu-His-Val residues of the 163 amino acid cytoplasmic tail of the bovine Man-6-P/IGF-II receptor partially impaired this function, resulting in the diversion of a portion of the receptor-ligand complexes to the cell surface, where they were endocytosed. The same phenotype was observed when 134 residues of the cytoplasmic tail were deleted from the carboxyl terminus. Disruption of the Tyr24-Lys-Tyr-Ser-Lys-Val29 plasma membrane internalization signal alone had little effect on Golgi sorting, but when combined with either deletion resulted in a complete loss of this function. The mutant receptors retained the ability to recycle to the Golgi and bind cathepsin D. These results indicate that the cytoplasmic tail of the Man-6-P/IGF-II receptor contains two signals that contribute to Golgi sorting, presumably by interacting with the Golgi clathrin-coated pit adaptor proteins. The Leu-Leu-containing sequence represents a novel motif for mediating interaction with Golgi adaptor proteins.

scholarly journals The Kangaroo Cation-independent Mannose 6-Phosphate Receptor Binds Insulin-like Growth Factor II with Low Affinity

1999 ◽  
Vol 274 (38) ◽  
pp. 27076-27082 ◽  
Author(s):  
Catherine A. Yandell ◽  
Andrew J. Dunbar ◽  
John F. Wheldrake ◽  
Zee Upton
Keyword(s):  
Growth Factor ◽  
Insulin Like Growth Factor ◽  
Factor Ii ◽  
Mannose 6 Phosphate

scholarly journals Dimerization of the Insulin-like Growth Factor II/Mannose 6-Phosphate Receptor

2000 ◽  
Vol 275 (25) ◽  
pp. 18647-18656 ◽  
Author(s):  
James C. Byrd ◽  
Jung H. Y. Park ◽  
Beverly S. Schaffer ◽  
Farideh Garmroudi ◽  
Richard G. MacDonald
Keyword(s):  
Growth Factor ◽  
Insulin Like Growth Factor ◽  
Factor Ii ◽  
Mannose 6 Phosphate
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