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A more recent version of this article appeared on March 1, 2004
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Submitted on August 18, 2003
Revised on November 24, 2003
Accepted on November 27, 2003
1 Department of Molecular Animal Physiology, Nijmegen Center for Molecular Life Sciences (NCMLS), University of Nijmegen, 6525 GA Nijmegen, The Netherlands
* Corresponding author. E-mail address: g.martens{at}ncmls.kun.nl.
The p24
, -
, -
and -
proteins are major multimeric constituents of cycling endoplasmic reticulum-Golgi transport vesicles and thought to be involved in protein transport through the early secretory pathway. In this study, we targeted transgene overexpression of p24
2 specifically to the Xenopus intermediate pituitary melanotrope cell that is involved in background adaptation of the animal and produces high levels of its major secretory cargo proopiomelanocortin (POMC). The transgene product effectively displaced the endogenous p24 proteins resulting in a melanotrope cell p24 system that consisted predominantly of the transgene p24
2 protein. Despite the severely distorted p24 machinery, the subcellular structures as well as the level of POMC synthesis were normal in these cells. However, the number and pigment content of skin melanophores were reduced, impairing the ability of the transgenic animal to fully adapt to a black background. This physiological effect was likely caused by the affected profile of POMC-derived peptides observed in the transgenic melanotrope cells. Together, our results suggest that in the early secretory pathway an intact p24 system is essential for efficient secretory cargo transport or for supplying cargo carriers with the correct protein machinery to allow proper secretory protein processing.
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