| dc.creator |
Postma, M |
|
| dc.creator |
Van Haastert, PJM |
|
| dc.creator |
Visser, AJWG |
|
| dc.creator |
Ruchira, Ruchira |
|
| dc.creator |
Roelofs, J |
|
| dc.creator |
Kortholt, Arjan |
|
| dc.creator |
Knol, JC |
|
| dc.creator |
Blaauw, M |
|
| dc.date |
2003-10-01T00:00:00Z |
|
| dc.date.accessioned |
2023-01-09T12:03:15Z |
|
| dc.date.available |
2023-01-09T12:03:15Z |
|
| dc.identifier |
5eaa31b9-d28b-41f5-a056-3384cddbce68 |
|
| dc.identifier |
10.1093/emboj/cdg508 |
|
| dc.identifier |
https://avesis.sdu.edu.tr/publication/details/5eaa31b9-d28b-41f5-a056-3384cddbce68/oai |
|
| dc.identifier.uri |
http://acikerisim.sdu.edu.tr/xmlui/handle/123456789/97906 |
|
| dc.description |
Retinal phosducin is known to sequester transducin Gbetagamma, thereby modulating transducin activity. Phos ducin is a member of a family of phosducin-like proteins (PhLP) found in eukaryotes. Phylogeny of 33 phosducin-like proteins from metazoa, plants and lower eukaryotes identified three distinct groups named phosducin-I-III. We discovered three phlp genes in Dictyostelium, each encoding a phosducin-like protein of a different group. Disruption of the phlp1 gene strongly impaired G-protein signalling, apparently due to mislocalization of Gbetagamma in phlp1-null cells. GFP-Gbeta and GFP-Ggamma are membrane associated in wild-type cells, but cytosolic in phlp1-null cells. Phlp2 disruption is lethal due to a synchronous collapse of the cells after 16-17 cell divisions. Phlp3 disruptants show no abnormal phenotype. These results establish a role for phosducin-like proteins in facilitating folding, localization or function of proteins, in addition to modulating G-protein signalling. |
|
| dc.language |
eng |
|
| dc.rights |
info:eu-repo/semantics/openAccess |
|
| dc.title |
Phosducin-like proteins in Dictyostelium discoideum: implications for the phosducin family of proteins |
|
| dc.type |
info:eu-repo/semantics/article |
|