The lysosomal trafficking regulator interacting protein-5 localizes mainly in epithelial cells |
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Authors: | Michelle Boone Ali Mobasheri Robert A Fenton Bas W M van Balkom Ronnie Wismans Catharina E E M van der Zee Peter M T Deen |
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Institution: | (1) Department of Physiology, Radboud University Nijmegen Medical Centre, Nijmegen, The Netherlands;(2) Division of Veterinary Medicine, School of Veterinary Medicine and Science, Faculty of Medicine and Health Sciences, University of Nottingham, Sutton Bonington Campus, Leicestershire, UK;(3) Water and Salt Research Centre, University of Aarhus, Aarhus, Denmark;(4) Department of Cell Biology, NCMLS, Radboud University Nijmegen Medical Centre, Nijmegen, The Netherlands;(5) Present address: Department of Nephrology and Hypertension, UMC Utrecht, Utrecht, The Netherlands;(6) 286 Physiology, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands; |
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Abstract: | Endocytosis, subsequent protein sorting into multivesicular bodies (MVBs), and eventual degradation in lysosomes compose an
important mechanism for controlling protein expression on the plasma membrane. The lysosomal trafficking regulator interacting
protein-5 (LIP5) is part of the complex protein machinery involved in MVB biosynthesis. LIP5 interacts with other players
of the ESCRT machinery as well as with two known cargo proteins, AQP2 and EGFR, whose degradation is affected upon reduction
of LIP5 expression. To investigate the expression and localization pattern of LIP5, we studied LIP5 protein expression in
a mouse tissue panel and subjected various rodent and human tissues to immunohistochemistry. Immunoblotting revealed that,
except for jejunum, LIP5 is expressed as a 42 kDa protein in all mouse tissues tested. Alternatively-spliced gene products
could not be detected. Immunohistochemical studies revealed that in tissues positive for LIP5, LIP5 is detected in virtually
all epithelial cells of the examined rodent and human tissues. The observed LIP5 expression in epithelial tissues suggests
that LIP5 is of particular importance in the MVB sorting and degradation of proteins expressed in polarized cells. |
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