title: Lumenal protein multimerization in the distal secretory pathway/secretory granules.
abstract: Differences in protein solubility appear to play an important role in lumenal protein trafficking through Golgi/post-Golgi compartments. Recent advances indicate that multimeric protein assembly is one of the factors regulating the efficiency of protein storage within secretory granules, by mechanisms that, with slight modification, might be considered to represent the culmination of a process of Golgi cisternal maturation.
authors.affiliation: Division of Endocrinology/Diabetes Center, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA. arvan@aecom.yu.edu
authors.forename: Peter
authors.initials: P
authors.lastname: Arvan
authors.forename: Bao-yan
authors.initials: BY
authors.lastname: Zhang
authors.forename: Lijun
authors.initials: L
authors.lastname: Feng
authors.forename: Ming
authors.initials: M
authors.lastname: Liu
authors.forename: Regina
authors.initials: R
authors.lastname: Kuliawat
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D002451:Cell Compartmentation; D003594:Cytoplasmic Granules / Q000378:metabolism* / Q000648:ultrastructure; D006056:Golgi Apparatus / Q000378:metabolism*; D006801:Humans; D007425:Intracellular Membranes / Q000378:metabolism; D008954:Models, Biological; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D021381:Protein Transport; D011506:Proteins / Q000378:metabolism*; D012995:Solubility; D021601:trans-Golgi Network / Q000378:metabolism
chemical_list: D002352:Carrier Proteins; D011498:Protein Precursors; D011506:Proteins