Lumenal protein sorting to the constitutive secretory pathway of a regulated secretory cell.

ABSTRACT: Newly synthesized secretory granule content proteins are delivered via the Golgi complex for storage within mature granules, whereas constitutive secretory proteins are not stored. Most soluble proteins traveling anterograde through the trans-Golgi network are not excluded from entering immature secretory granules, whether or not they have granule-targeting signals. However, the ;sorting-for-entry' hypothesis suggests that soluble lumenal proteins lacking signals enter transport intermediates for the constitutive secretory pathway. We aimed to investigate how these constitutive secretory proteins are sorted. In a pancreatic beta-cell line, we stably expressed two lumenal proteins whose normal sorting information has been deleted: alkaline phosphatase, truncated to eliminate its glycosylpho

SUBMITTER: Lara-Lemus R 

PROVIDER: S-EPMC2547412 | biostudies-literature | 2006 May

REPOSITORIES: biostudies-literature