Lipoprotein receptors and a Disabled family cytoplasmic adaptor protein regulate EGL-17/FGF export in C. elegans

Autor: Darren M. Kamikura, Jonathan A. Cooper
Jazyk: angličtina
Rok vydání: 2003
Předmět:
Cytoplasm
animal structures
Amino Acid Motifs
Green Fluorescent Proteins
Fluorescent Antibody Technique
Golgi Apparatus
Saccharomyces cerevisiae
Endocytosis
Fibroblast growth factor
Vulva
Cell Movement
Two-Hybrid System Techniques
Genetics
Animals
Gene Silencing
Receptor
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Secretory pathway
Adaptor Proteins
Signal Transducing
Receptors
Lipoprotein
biology
fungi
Signal transducing adaptor protein
biology.organism_classification
Phosphoproteins
Research Papers
Precipitin Tests
Transmembrane protein
Cell biology
Fibroblast Growth Factors
Adaptor Proteins
Vesicular Transport
Luminescent Proteins
Biochemistry
Mutation
Intercellular Signaling Peptides and Proteins
Clathrin adaptor proteins
lipids (amino acids
peptides
and proteins)
Female
Apoptosis Regulatory Proteins
Developmental Biology
Subcellular Fractions
Popis: Growth factors and morphogens need to be secreted to act on distant cells during development and in response to injury. Here, we report evidence that efficient export of a fibroblast growth factor (FGF), EGL-17, from the Caenorhabditis elegans developing vulva requires the lipoprotein receptor-related proteins Ce-LRP-1 and Ce-LRP-2 and a cytoplasmic adaptor protein, Ce-DAB-1 (Disabled). Lipoprotein receptors are transmembrane proteins best known for their roles in endocytosis. Ce-LRP-1 and Ce-LRP-2 possess a conserved intraluminal domain that can bind to EGL-17, as well as a cytosolic FXNPXY motif that can bind to Ce-DAB-1. Ce-DAB-1 contains signals that confer subcellular localization to Golgi-proximal vesicles. These results suggest a model in which Ce-DAB-1 coordinates selection of receptors and cargo, including EGL-17, for transport through the secretory pathway.
Databáze: OpenAIRE
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