000115126 001__ 115126
000115126 005__ 20181203021036.0
000115126 037__ $$aARTICLE
000115126 245__ $$aThe tyrosinase tail mediates sorting to the lysosomal compartment in MDCK cells via a di-leucine and a tyrosine-based signal
000115126 269__ $$a1999
000115126 260__ $$c1999
000115126 336__ $$aJournal Articles
000115126 520__ $$aTyrosinase is a type I membrane protein found in melanosomes, which are lysosomal-like organelles and specific for pigment cells. A mutation of mouse tyrosinase, platinum (cp), leads to truncation of tyrosinase's cytosolic tail, and results in misrouting to the cell periphery. In this study, we expressed chimeras of wild-type and mutant cytosolic tails of mouse tyrosinase fused to rat lysosome-associated membrane protein-1 luminal and transmembrane domain to study sorting of tyrosinase in Madin-Darby canine kidney cells. The study shows that the mouse tyrosinase cytosolic tail is necessary and sufficient to mediate sorting of a heterologous type I membrane protein to compartments of the lysosomal lineage. Whereas deletions of 7 or 10 C-terminal amino acids of the tail still result in sorting to lysosomes, a deletion mutant corresponding to platinum (cp) tail fails to sort correctly and corroborates the in situ findings in cp homozygous mutant mice. Correct sorting of tyrosinase-lysosome-associated membrane protein-1 chimeras is mediated by the interplay of a di-leucine signal and a tyrosine motif of the Y-X-X-O type.
000115126 700__ $$aSimmen, T.
000115126 700__ $$aSchmidt, A.
000115126 700__ $$aHunziker, W.
000115126 700__ $$g169239$$aBeermann, F.$$0240256
000115126 773__ $$j112$$tJournal of Cell Science$$kPt 1$$q45-53
000115126 909C0 $$xU11779$$0252092$$pGR-BEERMANN
000115126 909CO $$pSV$$particle$$ooai:infoscience.tind.io:115126
000115126 937__ $$aGR-BEERMANN-ARTICLE-1999-006
000115126 973__ $$rREVIEWED$$sPUBLISHED$$aOTHER
000115126 980__ $$aARTICLE