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Inactivation Of Lmpa, Encoding A Limpii-Related Endosomal Protein, Suppresses The Internalization And Endosomal Trafficking Defects In Profilin-Null Mutants, Lesly A. Temesvari, Linyi Zhang, Brent Fodera, Klaus-Peter Janssen, Michael Schleicher, James A. Caradelli

Publications

Profilin is a key phosphoinositide and actin-binding protein connecting and coordinating changes in signal transduction pathways with alterations in the actin cytoskeleton. Using biochemical assays and microscopic approaches, we demonstrate that profilin-null cells are defective in macropinocytosis, fluid phase efflux, and secretion of lysosomal enzymes but are unexpectedly more efficient in phagocytosis than wild-type cells. Disruption of the lmpA gene encoding a protein (DdLIMP) belonging to the CD36/LIMPII family suppressed, to different degrees, most of the profilin-minus defects, including the increase in F-actin, but did not rescue the secretion defect. Immunofluorescence microscopy indicated that DdLIMP, which is also capable of …