Dd-Alix, a conserved endosome-associated protein, controls Dictyostelium development
| Autor: | W. Jonathan Ryves, Laurence Aubry, Michel Satre, Sara Mattei, Béatrice Blot, Rémy Sadoul, Adrian J. Harwood, Gérard Klein |
|---|---|
| Přispěvatelé: | Biochimie et biophysique des systèmes intégrés (BBSI), Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Grenoble Institute of Neuroscience, Université Joseph Fourier - Grenoble 1 (UJF) |
| Jazyk: | angličtina |
| Rok vydání: | 2005 |
| Předmět: |
MESH: Sequence Homology
Amino Acid Endocytic cycle Protozoan Proteins MESH: Dictyostelium MESH: Amino Acid Sequence Conserved sequence Vps32 0302 clinical medicine MESH: Gene Expression Regulation Developmental Dictyostelium MESH: Animals Peptide sequence MESH: Protozoan Proteins Conserved Sequence Mammals 0303 health sciences MESH: Conserved Sequence biology Gene Expression Regulation Developmental Endocytosis Cell biology Alix Plasmids Endosome Molecular Sequence Data Morphogenesis MESH: Sequence Alignment Endosomes Development ESCRT MESH: Mammals 03 medical and health sciences MESH: Plasmids Animals Humans Biotinylation MESH: Biotinylation [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence Molecular Biology 030304 developmental biology MESH: Humans MESH: Molecular Sequence Data Sequence Homology Amino Acid Cell Biology biology.organism_classification Membrane protein MESH: Endosomes Sequence Alignment 030217 neurology & neurosurgery Developmental Biology |
| Zdroj: | Developmental Biology Developmental Biology, Elsevier, 2005, 279 (1), pp.99-113. ⟨10.1016/j.ydbio.2004.12.004⟩ Developmental Biology, 2005, 279 (1), pp.99-113. ⟨10.1016/j.ydbio.2004.12.004⟩ |
| ISSN: | 0012-1606 1095-564X |
| DOI: | 10.1016/j.ydbio.2004.12.004⟩ |
| Popis: | International audience; We have characterized the Dictyostelium homolog of the mammalian protein Alix. Dd-Alix is encoded by a single gene and is expressed during vegetative growth and multicellular development. We showed that the alx null strain fails to complete its developmental program. Past the tight aggregate stage, morphogenesis is impaired, leading to markedly aberrant structures containing vacuolated and undifferentiated cells but no mature spores. The developmental defect is cell-autonomous as most cells remain of the PstB type even when mixed with wild-type cells. Complementation analysis with different Alix constructs allowed the identification of a 101-residue stretch containing a coiled-coil domain essential for Alix function. In addition, we showed that the protein associates in part with vesicular structures and that its distribution on a Percoll gradient overlaps that of the endocytic marker Vamp7. Dd-Alix also co-localizes with Dd-Vps32. In view of our data, and given the role of Vps32 proteins in membrane protein sorting and multivesicular body formation in yeast and mammals, we hypothesize that the developmental defects of the alx null strain result from abnormal trafficking of cell-surface receptors. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect