Title: trans-Golgi retention of a plasma membrane protein: mutations in the cytoplasmic domain of the asialoglycoprotein receptor subunit H1 result in trans-Golgi retention Document date: 1995_7_2
ID: tedj3xxz_36
Snippet: Because conversion to the complex glycosylated form is slow, the half-lives of the mature wild-type and mutant proteins were determined using their sulfatable variants H1Ts and Hl(A4-33A) Ts which can be specifically labeled in their final forms with [35S]sulfate. The mature mutant protein has a half-life of ~5 h which is somewhat shorter than that of the wild-type H1Ts of ~7 h (Fig. 7 B) . In addition, inhibition of protein synthesis for 3.5 h w.....
Document: Because conversion to the complex glycosylated form is slow, the half-lives of the mature wild-type and mutant proteins were determined using their sulfatable variants H1Ts and Hl(A4-33A) Ts which can be specifically labeled in their final forms with [35S]sulfate. The mature mutant protein has a half-life of ~5 h which is somewhat shorter than that of the wild-type H1Ts of ~7 h (Fig. 7 B) . In addition, inhibition of protein synthesis for 3.5 h with 100 ixg/ ml cycloheximide did not change the distribution of Hl(A4-33A). Together these results argue against rapid missorting of Hl(A4-33A) to lysosomes with transient ac-cumulation in the Golgi, but rather suggest an efficient mechanism of retention of Hl(A4-33A) in the Golgi.
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