Enhancement of membrane insertion and function in a type IIIb membrane protein following introduction of a cleavable signal peptide.
XM Guan, TS Kobilka, BK Kobilka - Journal of Biological Chemistry, 1992 - ASBMB
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 …
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 …