Heat shock protein 47 (Hsp47) is an endoplasmic reticulum (ER)-resident molecular
chaperone essential for correct folding of procollagen in mammalian cells. In this Review …

The limited accessibility of bone and its mineralized nature have restricted deep
investigation of its biology. Recent breakthroughs in identification of mutant proteins …

Secretion and assembly of collagen are fundamental to the function of the extracellular
matrix. Defects in the assembly of a collagen matrix lead to pathologies including fibrosis …

Newly synthesized secretory proteins are exported from the endoplasmic reticulum (ER) at
specialized subcompartments called exit sites (ERES). Cargoes like procollagen are too …

Osteogenesis imperfecta (OI) is characterized primarily by susceptibility to fractures with or
without bone deformation. OI is genetically heterogeneous: over 20 genetic causes are …

As an essential step in conventional protein secretion, coat protein complex II (COP II)
mediates vesicular transport from the ER to the Golgi apparatus in eukaryotes. The GTPase …

Efficient quality control and export of procollagen from the cell is crucial for extracellular
matrix homeostasis, yet it is still incompletely understood. One of the debated questions is …

Collagen IV networks endow basement membranes (BMs) with remarkable tensile strength
and function as morphoregulatory substrata for diverse tissue-specific developmental …

Large coat protein complex II (COPII)-coated vesicles serve to convey the large cargo
procollagen I (PC1) from the endoplasmic reticulum (ER). The link between large cargo in …

The realization that the meticulous organization of cellular organelles is not required for the
reconstitution of select intracellular traffic steps has revolutionized cell biology. It transformed …