| Autor: |
Guan XM; Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University, California 94305., Kobilka TS, Kobilka BK |
| Jazyk: |
angličtina |
| Zdroj: |
The Journal of biological chemistry [J Biol Chem] 1992 Nov 05; Vol. 267 (31), pp. 21995-8. |
| Abstrakt: |
The human beta 2 adrenergic receptor is a type IIIb membrane protein. It has a putative seven-transmembrane topology but lacks an amino-terminal cleavable signal sequence. The mechanism by which the amino terminus of the beta 2 receptor is translocated across the endoplasmic reticulum membrane is unknown. Furthermore, it is not known if translocation as a type IIIb protein is essential for the proper folding. Our studies indicate that conversion of beta 2 receptor from a type IIIb to a type IIIa membrane protein by introducing an NH2-terminal cleavable signal sequence enhances translocation of the receptor into the endoplasmic reticulum membrane, thereby facilitating expression of functional receptor. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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