Publication year
2009Source
International Journal of Biochemistry & Cell Biology, 41, 7, (2009), pp. 1619-1627ISSN
Publication type
Article / Letter to editor

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Organization
Molecular Animal Physiology
Biochemistry (UMC)
Pulmonary Diseases
Journal title
International Journal of Biochemistry & Cell Biology
Volume
vol. 41
Issue
iss. 7
Page start
p. 1619
Page end
p. 1627
Subject
Molecular Animal Physiology; N4i 1: Pathogenesis and modulation of inflammation; NCMLS 3: Tissue engineering and pathology; NCMLS 6: Genetics and epigenetic pathways of diseaseAbstract
The p24 family is thought to be somehow involved in endoplasmic reticulum-to-Golgi protein transport, and its members are major constituents of transport vesicles and bind to the vesicle coat protein complexes COPI and COPII. A subset of the p24 proteins (p24alpha(3), -beta(1), -gamma(3) and -delta(2)) is upregulated when Xenopus laevis intermediate pituitary melanotrope cells are physiologically activated to produce vast amounts of their major secretory cargo, the prohormone proopiomelanocortin (POMC). To investigate the role of the COP-binding motifs of p24 proteins in POMC biosynthesis, we here generated and analysed Xenopus with stable, melanotrope cell-specific transgene expression of p24delta(2)-GFP mutated in its COPI- or COPII-binding motif. In contrast to what has been found previously for wild-type (wt) p24delta(2)-GFP, the p24delta(2) mutations prevented the Golgi localisation of the transgene products and caused a reduced rate of POMC cleavage, but did not lead to a reduction of the endogenous p24 proteins nor to aberrations in POMC glycosylation and sulphation. We conclude that p24delta(2) requires the presence of the COPI- and COPII-binding sites to allow proper POMC processing. Thus, the p24 proteins fulfil their role in secretory protein biosynthesis via COPI- or COPII-coated transport vesicles.
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- Faculty of Medical Sciences [81051]
- Faculty of Science [32345]
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