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J Biol Chem, Vol. 274, Issue 43, 30550-30556, October 22, 1999
,,
From the The effect of protein kinase inhibitors on
transferrin receptor (TR) internalization was examined in HeLa, A431,
3T3-L1 cells, and primary chicken embryo fibroblasts. We show that TR
endocytosis is not affected by tyrosine kinase or protein kinase C
inhibitors, but is inhibited by one serine/threonine kinase inhibitor,
H-89. Inhibition occurred within 15 min, was completely reversible
after H-89 withdrawal, and was specific for endocytosis rather than pinocytosis since a TR mutant lacking an internalization signal was not
affected. Interestingly, H-89 also inhibited the internalization of a
TR chimera containing the major histocompatibility complex class II
invariant chain cytoplasmic tail, indicating that the effect was not
specific for the TR. Since H-89 inhibits a number of kinases, we
employed a permeabilized cell endocytosis assay to further characterize
the kinase. In permeabilized 3T3-L1 cells, addition of pseudosubstrate
inhibitor peptides of casein kinase II (CKII) blocked TR
internalization by more than 50%, whereas pseudosubstrates of cyclic
AMP-dependent kinase A, protein kinase C, and casein kinase
I had no effect. Furthermore, addition of purified CKII to the
cell-free reactions containing CKII pseudosubstrates reversed the
endocytosis block, suggesting that CKII or a CKII-like activity is
required for constitutive endocytosis.
Department of Cell Biology, University of
Alabama at Birmingham, MCLM 392, UAB Station, Birmingham, Alabama
35294-0005 and the § Department of Cell Biology, The Scripps
Research Institute, La Jolla, California 92037
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