1. ZHAW digitalcollection
  2. Life Sciences und Facility Management
  3. Publikationen
  4. Publikationen Life Sciences und Facility Management
Full metadata record
DC FieldValueLanguage
dc.contributor.authorSchweizer, Anja-
dc.contributor.authorKornfeld, Stuart-
dc.contributor.authorRohrer, Jack-
dc.date.accessioned2018-06-13T09:30:31Z-
dc.date.available2018-06-13T09:30:31Z-
dc.date.issued1996-02-15-
dc.identifier.issn0021-9525de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/6829-
dc.description.abstractWe have examined whether the two cysteine residues (Cys30 and Cys34) in the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor are palmitoylated via thioesters and whether these residues influence the biologic function of the receptor. To do this, mouse L cells expressing wild-type and mutant receptors were analyzed by metabolic labeling with [3H]palmitate, immunoprecipitation, and SDS-PAGE. Both Cys30 and Cys34 were found to be sites of palmitoylation and together they accounted for the total palmitoylation of the receptor. The palmitate rapidly turned over with a half-life of approximately 2 h compared to a half-life of greater than 40 h for the protein. Mutation of Cys34 to Ala resulted in the gradual accumulation of the receptor in dense lysosomes and the total loss of cathepsin D sorting function in the Golgi. A Cys30 to Ala mutation had no biologic consequences, showing the importance of Cys34. Mutation of amino acids 35-39 to alanines impaired palmitoylation of Cys30 and Cys34 and resulted in abnormal receptor trafficking to lysosomes and loss of cathepsin D sorting. These data suggest that palmitoylation of Cys30 and Cys34 leads to anchoring of this region of the cytoplasmic tail to the lipid bilayer. Anchoring via Cys34 is essential for the normal trafficking and lysosomal enzyme sorting function of the receptor.de_CH
dc.language.isoende_CH
dc.publisherRockefeller University Pressde_CH
dc.relation.ispartofJournal of Cell Biologyde_CH
dc.rightsLicence according to publishing contractde_CH
dc.subject.ddc572: Biochemiede_CH
dc.titleCysteine34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sortingde_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
dc.identifier.doi10.1083/jcb.132.4.577de_CH
zhaw.funding.euNode_CH
zhaw.issue4de_CH
zhaw.originated.zhawYesde_CH
zhaw.pages.end584de_CH
zhaw.pages.start577de_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume132de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
Appears in collections:Publikationen Life Sciences und Facility Management

Files in This Item:
There are no files associated with this item.
Show simple item record
Schweizer, A., Kornfeld, S., & Rohrer, J. (1996). Cysteine34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting. Journal of Cell Biology, 132(4), 577–584. https://doi.org/10.1083/jcb.132.4.577
Schweizer, A., Kornfeld, S. and Rohrer, J. (1996) ‘Cysteine34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting’, Journal of Cell Biology, 132(4), pp. 577–584. Available at: https://doi.org/10.1083/jcb.132.4.577.
A. Schweizer, S. Kornfeld, and J. Rohrer, “Cysteine34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting,” Journal of Cell Biology, vol. 132, no. 4, pp. 577–584, Feb. 1996, doi: 10.1083/jcb.132.4.577.
SCHWEIZER, Anja, Stuart KORNFELD und Jack ROHRER, 1996. Cysteine34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting. Journal of Cell Biology. 15 Februar 1996. Bd. 132, Nr. 4, S. 577–584. DOI 10.1083/jcb.132.4.577
Schweizer, Anja, Stuart Kornfeld, and Jack Rohrer. 1996. “Cysteine34 of the Cytoplasmic Tail of the Cation-Dependent Mannose 6-Phosphate Receptor Is Reversibly Palmitoylated and Required for Normal Trafficking and Lysosomal Enzyme Sorting.” Journal of Cell Biology 132 (4): 577–84. https://doi.org/10.1083/jcb.132.4.577.
Schweizer, Anja, et al. “Cysteine34 of the Cytoplasmic Tail of the Cation-Dependent Mannose 6-Phosphate Receptor Is Reversibly Palmitoylated and Required for Normal Trafficking and Lysosomal Enzyme Sorting.” Journal of Cell Biology, vol. 132, no. 4, Feb. 1996, pp. 577–84, https://doi.org/10.1083/jcb.132.4.577.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.