| Autor: |
Jacobsen L; Department of Molecular and Cellular Neurobiology, Vrije Universiteit, 1081 HV Amsterdam, The Netherlands. lija@bio.vu.nl, Madsen P, Nielsen MS, Geraerts WP, Gliemann J, Smit AB, Petersen CM |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 2002 Jan 30; Vol. 511 (1-3), pp. 155-8. |
| DOI: |
10.1016/s0014-5793(01)03299-9 |
| Abstrakt: |
We report that the Vps10p domain receptor sorLA binds the adaptor proteins GGA1 and -2, which take part in Golgi-endosome sorting. The GGAs bind with differential requirements via three critical residues in the C-terminal segment of the sorLA cytoplasmic tail. Unlike in sortilin and the mannose 6-phosphate receptors, the GGA-binding segment in sorLA contains neither an acidic cluster nor a dileucine. Our results support the concept of sorLA as a potential sorting receptor and suggest that key residues in sorLA and sortilin conform to a new type of motif (psi-psi-X-X-phi) defining minimum requirements for GGA binding to cytoplasmic receptor domains. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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