TY - JOUR
T1 - Dissecting functions of the retinoblastoma tumor suppressor and the related pocket proteins by integrating genetic, cell biology, and electrophoretic techniques.
AU - Hansen, Klaus
AU - Lukas, J
AU - Holm, K
AU - Kjerulff, A A
AU - Bartek, J
N1 - Keywords: Amino Acid Sequence; Animals; Electrophoresis, Gel, Two-Dimensional; Electrophoresis, Polyacrylamide Gel; Female; Genes, Tumor Suppressor; Humans; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Nuclear Proteins; Phosphoproteins; Proteins; Retinoblastoma Protein; Retinoblastoma-Like Protein p107; Retinoblastoma-Like Protein p130; Tumor Cells, Cultured
PY - 1999
Y1 - 1999
N2 - The members of the 'pocket protein' family, comprising the retinoblastoma tumor suppressor (pRB) and its relatives, p107 and p130, negatively regulate cell proliferation and modulate fundamental biological processes including embryonic development, differentiation, homeostatic tissue renewal, and defense against cancer. The large, multidomain pocket proteins act by binding a plethora of cell fate-determining and growth-stimulatory proteins, the most prominent of which are the E2F/DP transcription factors. These protein-protein interactions are in turn regulated by carefully orchestrated phosphorylation events on multiple serine and threonine residues of pRB, p107, and p130, events which are carried out, at least in part, by the cyclin-dependent kinases that form the key elements of the cell cycle machinery. Here we discuss the recently obtained new insights into the diverse functions of the pRB family, and show examples of how integration of genetic, cell biology, and a range of electrophoretic approaches help to advance our understanding of the biological roles played by the pocket proteins in both normal and cancer cells.
AB - The members of the 'pocket protein' family, comprising the retinoblastoma tumor suppressor (pRB) and its relatives, p107 and p130, negatively regulate cell proliferation and modulate fundamental biological processes including embryonic development, differentiation, homeostatic tissue renewal, and defense against cancer. The large, multidomain pocket proteins act by binding a plethora of cell fate-determining and growth-stimulatory proteins, the most prominent of which are the E2F/DP transcription factors. These protein-protein interactions are in turn regulated by carefully orchestrated phosphorylation events on multiple serine and threonine residues of pRB, p107, and p130, events which are carried out, at least in part, by the cyclin-dependent kinases that form the key elements of the cell cycle machinery. Here we discuss the recently obtained new insights into the diverse functions of the pRB family, and show examples of how integration of genetic, cell biology, and a range of electrophoretic approaches help to advance our understanding of the biological roles played by the pocket proteins in both normal and cancer cells.
U2 - 10.1002/(SICI)1522-2683(19990201)20:2<372::AID-ELPS372>3.0.CO;2-R
DO - 10.1002/(SICI)1522-2683(19990201)20:2<372::AID-ELPS372>3.0.CO;2-R
M3 - Journal article
C2 - 10197445
SN - 0173-0835
VL - 20
SP - 372
EP - 381
JO - Electrophoresis
JF - Electrophoresis
IS - 2
ER -
