TAILIEUCHUNG - Báo cáo khoa học: Misfolded endoplasmic reticulum retained subunits cause degradation of wild-type subunits of arylsulfatase A heteromers

Arylsulfatase A is an oligomeric lysosomal enzyme. In the present study, we use this enzyme as a model protein to examine how heteromerization of wild-type and misfolded endoplasmic reticulum-degraded arylsulfatase A polypeptides affects the quality control of wild-type arylsulfatase A subun-its. | Misfolded endoplasmic reticulum retained subunits cause degradation of wild-type subunits of arylsulfatase A heteromers Peter Poeppel1 Mekky Mohamed Abouzied1 2 Christof Volker1 and Volkmar Gieselmann1 1 Institut fur Biochemie und Molekularbiologie Rheinische-Friedrich-Wilhelms Universitat Bonn Germany 2 Faculty of Pharmacy University of El-Minia Egypt Keywords arylsulfatase A ERAD MLD protein oligomerization protein quality control Correspondence V. Gieselmann Institut fur Biochemie und Molekularbiologie Rheinische-Friedrich-Wilhelms Universitat Bonn Nussallee 11 53115 Bonn Germany Fax 49 228 732416 Tel 49 228 732411 E-mail gieselmann@ Present address Institut fCur Biochemie Universitat zu Koln Germany Arylsulfatase A is an oligomeric lysosomal enzyme. In the present study we use this enzyme as a model protein to examine how heteromerization of wild-type and misfolded endoplasmic reticulum-degraded arylsulfatase A polypeptides affects the quality control of wild-type arylsulfatase A subunits. Using a conformation sensitive monoclonal antibody we show that within heteromers of misfolded and wild-type arylsulfatase A the wild-type subunits are not fully folded. The results obtained show that arylsulfatase A polypeptide complexes rather than the monomers are subject to endoplasmic reticulum quality control and that within a heteromer the misfolded subunit exerts a dominant negative effect on the wild-type subunit. Although it has been shown that mature lysosomal arylsulfatase A forms dimers at neutral pH the results obtained in the present study demonstrate that in the early biosynthetic pathway arylsulfatase A forms oligomers with more than two subunits. Received 10 February 2010 revised 6 May 2010 accepted 18 June 2010 doi Introduction Many proteins form homooligomers. According to crystallization and in vitro gel filtration data the lysosomal enzyme arylsulfatase A ASA UniProt accession number P15289 forms dimers at

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