Identification of a novel prohormone sorting signal-binding site on carboxypeptidase E, a regulated secretory pathway-sorting receptor

Molecular Endocrinology

Volumn 13, Issue 4, 1999, Pages 527-536

  Zhang, Chun Fa ^a   Snell, Christopher R ^b   Loh, Y Peng ^a,c  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^b Novartis Inst for Medical Research   (United Kingdom)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; ARGININE; ASPARTIC ACID; CARBOXYPEPTIDASE H; GLUTAMIC ACID; HORMONE PRECURSOR; LEUCINE; LYSINE; PROENKEPHALIN; PROINSULIN; SERINE;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BACULOVIRUS; BINDING AFFINITY; CELL SELECTION; MOLECULAR INTERACTION; MOLECULAR MODEL; MUTATION; NONHUMAN; PRIORITY JOURNAL; SIGNAL TRANSDUCTION;

ANIMALIA; UNIDENTIFIED BACULOVIRUS;

EID: 0033330659     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/mend.13.4.0267     Document Type: Article

References (28)

1. The trans-most cisternae of the Golgi complex: A compartment for sorting of secretory and plasma membrane proteins
2. Proteolytic processing of pro-ACTH/endorphin begins in the Golgi complex of pituitary corticotropes and AtT20 cells
3. Carboxypeptidase E is a regulated secretory pathway sorting receptor: Genetic obliteration leads to endocrine disorders in Cpe(fat) mice
4. Receptor-mediated targeting of hormones to secretory granules: Role of carboxypeptidase E
5. Identification of a sorting signal for the regulated secretory pathway at the N-terminus of pro-opiomelanocortin
6. Identification of the sorting signal motif within pro-opiomelanocortin for the regulated secretory pathway
7. Carboxypeptidase E is a sorting receptor for prohormones: Binding and kinetic studies
8. Depletion of carboxypeptidase E, a regulated secretory pathway sorting receptor, causes misrouting and constitutive secretion of proinsulin and proenkephalin, but not chromogranin A
9. Intracellular misrouting and abnormal secretion of adrenocorticotropin and growth hormone in the Cpe(fat) mouse associated with a carboxypeptidase E mutation
10. Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity
11. Altered processing of procholecystokinin in carboxypeptidase E-deficient fat mice: Differential synthesis in neurons and endocrine cells
12. The structure of 2Zn pig insulin crystals at 1.5 Angstrom resolution
13. NMR and photo-CIDNP studies of human pro-insulin and prohormone processing intermediates with application to endopeptidase recognition
14. 202 of carboxypeptidase E
15. Chloroquine diverts ACTH from a regulated to a constitutive secretory pathway in AtT-20 cells
16. Rat preprocarboxypeptidase H
17. Differential distribution of carboxypeptidase-processing enzyme activity and immunoreactivity in membrane and soluble components of chromaffin granules
18. Carboxypeptidase E
19. β-Cell lines derived from transgenic Cpe(fat)/Cpe(fat) mice are defective in carboxypeptidase E and proinsulin processing
20. Proinsulin targeting to the regulated pathway is not impaired in carboxypeptidase E-deficient Cpe(fat)/Cpe(fat) mice
21. The pro region is not required for the expression or intracellular routing of carboxypeptidase E
22. Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its missorting to the constitutive secretory pathway
23. The disulfide bond in chromogranin B, which is essential for its sorting to secretory granules, is not required for its aggregation in the trans-Golgi network
24. The isoforms of proprotein convertase PC5 are sorted to different subcellular compartments
25. Identification of a transferable sorting domain for the regulated pathway in the prohormone convertase PC2
26. Identification of routing determinants in the cytosolic domain of a secretory granule-associated integral membrane protein
27. Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH
28. 1-33) is dictated by three disulfide bridges