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Mannose 6‐phosphate‐independent Lysosomal Sorting of LIMP ‐2
Author(s) -
Blanz Judith,
Zunke Friederike,
Markmann Sandra,
Damme Markus,
Braulke Thomas,
Saftig Paul,
Schwake Michael
Publication year - 2015
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12313
Subject(s) - limp , biology , microbiology and biotechnology , biochemistry , lysosome , bioinformatics , enzyme
The widely accepted view that β‐glucocerebrosidase ( GC ) is targeted to lysosomes by the lysosomal integral membrane protein type 2 ( LIMP ‐2) independent of the mannose 6‐phosphate ( M6P ) pathway has been recently challenged by the identification of a putative M6P residue in the crystalized LIMP ‐2 ectodomain. We demonstrate that LIMP ‐2 and GC reach lysosomes independent of the M6P pathway in fibroblasts and in purified liver lysosomes. Additionally, LIMP ‐2 could not be affinity‐purified using M6P ‐specific antibodies. Our data prove M6P ‐independent lysosomal sorting of LIMP ‐2 and GC .