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Identification of the nuclear localization signal of p21 cip1 and consequences of its mutation on cell proliferation
Author(s) -
Rodrı́guez-Vilarrupla Aina,
Dı́az Carmen,
Canela Núria,
Rahn Hans-Peter,
Bachs Oriol,
Agell Neus
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03549-4
Subject(s) - transfection , nuclear localization sequence , cell cycle , mutation , cell cycle checkpoint , mutant , nuclear export signal , amino acid , microbiology and biotechnology , fusion protein , nuclear transport , cell growth , nuclear protein , chromosomal translocation , biology , cell , chemistry , cell nucleus , cell culture , gene , genetics , cytoplasm , recombinant dna , transcription factor
Overexpression of p21 cip1 induces cell cycle arrest. Although this ability has been correlated with its nuclear localization, the evidence is not conclusive. The mutants that were used to inhibit its nuclear translocation could no longer bind to several proteins known to interact with the last 25 amino acids of p21 cip1 . Here we used point mutation analysis and fusion of the proteins to DsRed to identify which amino acids are essential for the nuclear localization of p21 cip1 . We conclude that amino acids RKR 140–142 are essential for nuclear translocation of p21 cip1 . While wild‐type DsRed‐p21 induces cell cycle arrest in 95% of transfected cells, overexpression of cytoplasmatic p21AAA 140–142 arrested only 20% of transfected cells. We conclude that cytoplasmatic p21, with no deletion in the C‐terminal region, had a much lower capacity to arrest the cell cycle.