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Endocrinopathies in the Family of Endoplasmic Reticulum (ER) Storage Diseases: Disorders of Protein Trafficking and the Role of ER Molecular Chaperones*

Division of Endocrinology (P.S.K.), University of Cincinnati College of Medicine, Cincinnati, Ohio 45267; and Division of Endocrinology (P.A.) and Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York 10461

Correspondence: Address correspondence to: Peter Arvan, M.D., Ph.D., Division of Endocrinology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461.

I. Introduction

A. Overview

B. Protein folding in the ER

C. Supervised folding: the concept of molecular chaperones and folding catalysts

D. Co- and posttranslational modifications are factors that can influence folding

II. ER Molecular Chaperones, Folding Catalysts, and Molecular Escorts

A. Binding protein (BiP)

B. GRP94

C. Calnexin and calreticulin

D. Disulfide isomerase and prolyl isomerase: families of folding catalysts

E. ERp72 and ER60

F. HSP47

G. Molecular escorts: pro-peptides, transport subunits, receptor-associated protein (RAP), and 7B2

III. Models of ER to Golgi Traffic Influence Models of Quality Control

A. Escape from ER retention as one hypothesis to explain anterograde protein traffic from the ER

B. Cargo receptors as another hypothesis to explain anterograde protein traffic from the ER

C. What provides quality control of ER export?

D. ER-associated degradation

IV. Endocrinopathies as Models of Defective Protein Export

A. Congenital hypothyroid goiter with thyroglobulin deficiency

B. Familial neurohypophyseal diabetes insipidus

C. Osteogenesis imperfecta and disorders of procollagen biosynthesis

D. ERSDs affecting lipoprotein metabolism

E. Other selected nonendocrine and endocrine ERSDs

V. Summary: A Proposed Classification of ERSDs