Identification of in vivo phosphorylation sites for basic-directed kinases in murine mdr1b P-glycoprotein by combination of mass spectrometry and site-directed mutagenesis

Methods Enzymol. 1998:292:342-58. doi: 10.1016/s0076-6879(98)92027-4.
No abstract available

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • ATP Binding Cassette Transporter, Subfamily B, Member 1 / biosynthesis
  • ATP Binding Cassette Transporter, Subfamily B, Member 1 / chemistry*
  • ATP Binding Cassette Transporter, Subfamily B, Member 1 / metabolism*
  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Chromatography, High Pressure Liquid / methods
  • Cloning, Molecular / methods
  • Cyanogen Bromide
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Drug Resistance, Multiple
  • Electrophoresis, Polyacrylamide Gel / methods
  • Macrophages
  • Mice
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Peptide Fragments / chemistry
  • Peptide Fragments / isolation & purification
  • Peptide Mapping / methods
  • Phosphopeptides / chemistry
  • Phosphopeptides / isolation & purification
  • Phosphorylation
  • Protein Engineering / methods
  • Protein Kinase C / metabolism*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Spectrometry, Mass, Secondary Ion / methods
  • Vinblastine / pharmacokinetics
  • Vinblastine / toxicity*

Substances

  • ATP Binding Cassette Transporter, Subfamily B, Member 1
  • Peptide Fragments
  • Phosphopeptides
  • Recombinant Proteins
  • Vinblastine
  • Cyclic AMP-Dependent Protein Kinases
  • Protein Kinase C
  • Cyanogen Bromide