Biogenesis of the protein storage vacuole crystalloid.
We identify new organelles associated with the vacuolar system in plant cells. These organelles are defined biochemically by their internal content of three integral membrane proteins: a chimeric reporter protein that moves there directly from the ER; a specific tonoplast intrinsic protein; and a novel receptor-like RING-H2 protein that traffics through the Golgi apparatus. Highly conserved homologues of the latter are expressed in animal cells. In a developmentally regulated manner, the organelles are taken up into vacuoles where, in seed protein storage vacuoles, they form a membrane-containing crystalloid. The uptake and preservation of the contents of these organelles in vacuoles represents a unique mechanism for compartmentalization of protein and lipid for storage.
Jiang
L
L
Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340, USA.
Phillips
T E
TE
Rogers
S W
SW
Rogers
J C
JC
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics / Q000502:physiology; D017124:Conserved Sequence; D019662:Cucurbitaceae / Q000502:physiology; D004721:Endoplasmic Reticulum / Q000502:physiology; D006056:Golgi Apparatus / Q000502:physiology; D008969:Molecular Sequence Data; D015388:Organelles / Q000502:physiology* / Q000648:ultrastructure; D010940:Plant Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D010944:Plants / Q000648:ultrastructure*; D030821:Plants, Genetically Modified; D011993:Recombinant Fusion Proteins / Q000032:analysis; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014617:Vacuoles / Q000502:physiology* / Q000648:ultrastructure
D010940:Plant Proteins; D011993:Recombinant Fusion Proteins