The molecular basis of oculocutaneous albinism type 1 (OCA1): Sorting failure and degradation of mutant tyrosinases results in a lack of pigmentation

Biochemical Journal

Volumn 355, Issue 2, 2001, Pages 259-269

  Toyofuku, K ^a   Wada, I ^a   Spritz, R A ^a   Hearing, V J ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Calnexin; Mutant protein; Protein transport

Indexed keywords

BIODEGRADATION; ENZYMES; GENES;

MUTATIONS;

DISEASES;

CALNEXIN; GLYCOSIDASE; MONOPHENOL MONOOXYGENASE; MUTANT PROTEIN;

ANIMAL CELL; ARTICLE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME LOCALIZATION; GENE MUTATION; MELANOSOME; NONHUMAN; OCULOCUTANEOUS ALBINISM; PHENOTYPE; PIGMENTATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN TARGETING; PROTEIN TRANSPORT; TEMPERATURE SENSITIVITY;

ALBINISM, OCULOCUTANEOUS; ANIMALS; CALCIUM-BINDING PROTEINS; CALNEXIN; COS CELLS; CYSTEINE ENDOPEPTIDASES; CYSTEINE PROTEINASE INHIBITORS; ENDOPLASMIC RETICULUM; HUMANS; HYDROLYSIS; IMMUNOHISTOCHEMISTRY; MONOPHENOL MONOOXYGENASE; MULTIENZYME COMPLEXES; PIGMENTATION; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN TRANSPORT; SUBCELLULAR FRACTIONS; TEMPERATURE;

EID: 0035871219     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3550259     Document Type: Article

References (48)

1. Genetic disorders of pigmentation
2. Abnormalities of pigmentation
3. Detection of mutations in the tyrosinase gene in a patient with Type IA oculocutaneous albinism
4. Molecular basis of albinism: Mutations and polymorphisms of pigmentation genes associated with albinism
5. Temperature-sensitive tyrosinase associated with peripheral pigmentation in oculocutaneous albinism
6. Mutational mapping of the catalytic activities of human tyrosinase
7. Non-random distribution of missense mutations within the human tyrosinase gene in Type 1 (tyrosinase-related) oculocutaneous albinism
8. Analysis of tyrosinase mutations associated with tyrosinase-related oculocutaneous albinism (OCA1)
9. Mutational analysis of copper-binding by human tyrosinase
10. Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP
11. Functional expression of the Wilson disease protein reveals mislocalization and impaired copper-dependent trafficking of the common H1069Q mutation
12. Association of folding intermediates of glycoproteins with calnexin during protein maturation
13. Calnexin: A membrane-bound chaperone of the endoplasmic reticulum
14. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
15. Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate
16. Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin
17. The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins
18. Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment
19. Degradation of a mutant secretory protein, alphal-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity
20. Proteasome-mediated degradation of apolipoprotein B targets both nascent peptides cotranslationally before translocation and full-length apolipoprotein B after translocation into the endoplasmic reticulum
21. Promotion of tyrosinase folding in Cos7 cells by calnexin
22. A common temperature-sensitive allelic form of human tyrosinase is retained in the endoplasmic reticulum at the nonpermissive temperature
23. Endoplasmic reticulum retention is a common defect associated with tyrosinase-negative albinism
24. Oligosaccharide trimming plays a role in the endoplasmic reticulum-associated degradation of tyrosinase
25. Tyrosinase folding and copper loading in vivo: A crucial role for calnexin and a-glucosidase II
26. Mutations at critical N-glycosylation sites reduce tyrosinase activity by altering folding and quality control
27. Tyrosinase and glycoprotein folding: Roles of chaperones that recognize glycans
28. Does tyrosinase exist in neuromelanin-pigmented neurons in the human substantia nigra?
29. Induction of pigmentation in mouse fibroblasts by expression of human tyrosinase cDNA
30. A cytoprasmic sequence in human tyrosinase defines a second class of dieucine-based sorting signals for late endosomar and lysosomal delivery
31. Melanosomes ate specialized members of the lysosomal lineage of organelles
32. Lysosomal hydrolases are present in melanosomes and are elevated in melanizing cells
33. ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together
34. Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells
35. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
36. Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cervisiae
37. High-molecular-weight forms of tyrosinase and the tyrosinase-related proteins: Evidence for a melanogenic complex
38. Tyrosinase stabilization by Tyrp1 (the brown locus protein)
39. Inhibition of N-glycan processing in B16 melanoma cells results in inactivation of tyrosinase but does not prevent its transport to the melanosome
40. The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
41. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
42. Mutant analysis links the translocon and BiP to retrograde protein transport for EFi degradation
43. Inhibition of glucose trimming with castanospermine reduces carnexin association and promotes proteasome degradation of the alpha-subunit of the nicotinic acetylcholine receptor
44. Mannose trimming targets mutant alpha(2)-plasmin inhibitor for degradation by the proteasome
45. The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
46. BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y fording in yeast
47. Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure
48. Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome