Masking of an endoplasmic reticulum retention signal by its presence in the two subunits of the asialoglycoprotein receptor
M Shenkman, M Ehrlich, GZ Lederkremer - Journal of Biological Chemistry, 2000 - ASBMB
Human asialoglycoprotein receptor H1 and H2b subunits assemble into a hetero-oligomer
that travels to the cell surface. The H2a variant on the other hand is a precursor of a cleaved
soluble form that is secreted. Uncleaved H2a precursor molecules cannot exit the
endoplasmic reticulum (ER), a lumenal juxtamembrane pentapeptide being responsible for
their retention. Insertion of this pentapeptide into H1 (H1i5) causes its complete ER retention
but not fast degradation as happens to H2a. Cotransfection of H2a elicited, by …
that travels to the cell surface. The H2a variant on the other hand is a precursor of a cleaved
soluble form that is secreted. Uncleaved H2a precursor molecules cannot exit the
endoplasmic reticulum (ER), a lumenal juxtamembrane pentapeptide being responsible for
their retention. Insertion of this pentapeptide into H1 (H1i5) causes its complete ER retention
but not fast degradation as happens to H2a. Cotransfection of H2a elicited, by …
