‘Piggy-Back' Transport of Xenopus Hyaluronan Synthase (XHAS1) via the Secretory Pathway to the Plasma Membrane

Verfasser / Beitragende:
[J. Müllegger, A. Rustom, G. Kreil, H.-H. Gerdes, G. Lepperdinger]
Ort, Verlag, Jahr:
2003
Enthalten in:
Biological Chemistry, 384/1(2003-01-27), 175-182
Format:
Artikel (online)
ID: 37884959X
LEADER caa a22 4500
001 37884959X
003 CHVBK
005 20180305123320.0
007 cr unu---uuuuu
008 161128e20030127xx s 000 0 eng
024 7 0 |a 10.1515/BC.2003.019  |2 doi 
035 |a (NATIONALLICENCE)gruyter-10.1515/BC.2003.019 
245 0 0 |a ‘Piggy-Back' Transport of Xenopus Hyaluronan Synthase (XHAS1) via the Secretory Pathway to the Plasma Membrane  |h [Elektronische Daten]  |c [J. Müllegger, A. Rustom, G. Kreil, H.-H. Gerdes, G. Lepperdinger] 
520 3 |a Hyaluronan is the sole glycosaminoglycan whose biosynthesis takes place directly at the plasma membrane. The mechanism by which hyaluronan synthase (HAS) becomes inserted there, as well as the question of how the enzyme discriminates between particular membrane species in polarized cells, are largely unknown. In vitro translation of HAS suggested that the nascent protein becomes stabilized in the presence of microsomal membranes, but would not insert spontaneously into membranes after being translated in the absence of those. We therefore monitored the membrane attachment of enzymatically active fusion proteins consisting of Xenopus HAS1 and green fluorescent protein shortly after de novo synthesis in Vero cells. Our data strongly suggest that HAS proteins are directly translated on the ER membrane without exhibiting an N-terminal signal sequence. From there the inactive protein is transferred to the plasma membrane via the secretory pathway. For unknown reasons, HAS inserted into membranes other than the plasma membrane remains inactive. 
540 |a Copyright © 2003 by Walter de Gruyter GmbH & Co. KG 
690 7 |a Biochemistry  |2 nationallicence 
690 7 |a Molecular biology  |2 nationallicence 
690 7 |a Cellular biology  |2 nationallicence 
700 1 |a Müllegger  |D J.  |4 aut 
700 1 |a Rustom  |D A.  |4 aut 
700 1 |a Kreil  |D G.  |4 aut 
700 1 |a Gerdes  |D H.-H  |4 aut 
700 1 |a Lepperdinger  |D G.  |4 aut 
773 0 |t Biological Chemistry  |d Walter de Gruyter  |g 384/1(2003-01-27), 175-182  |x 1431-6730  |q 384:1<175  |1 2003  |2 384  |o bchm 
856 4 0 |u https://doi.org/10.1515/BC.2003.019  |q text/html  |z Onlinezugriff via DOI 
908 |D 1  |a research article  |2 jats 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1515/BC.2003.019  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Müllegger  |D J.  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Rustom  |D A.  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Kreil  |D G.  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Gerdes  |D H.-H  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Lepperdinger  |D G.  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Biological Chemistry  |d Walter de Gruyter  |g 384/1(2003-01-27), 175-182  |x 1431-6730  |q 384:1<175  |1 2003  |2 384  |o bchm 
900 7 |b CC0  |u http://creativecommons.org/publicdomain/zero/1.0  |2 nationallicence 
898 |a BK010053  |b XK010053  |c XK010000 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-gruyter