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Cited by 507

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Subunit rearrangement of the cyclin-dependent kinases is associated with cellular transformation.

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Xiong, Y, Zhang, H, Beach, D·1993·Genes & Development

Abstract

In normal human diploid fibroblasts, cyclins of the A, B, and D classes each associate with cyclin-dependent kinases (CDKs), proliferating cell nuclear antigen (PCNA), and p21, thereby forming multiple independent quaternary complexes. Upon transformation of diploid fibroblasts with the DNA tumor virus SV40, or its transforming tumor antigen (T), the cyclin D/p21/CDK/PCNA complexes are disrupted. In transformed cells, CDK4 totally dissociates from cyclin D, PCNA, and p21 and, instead, associates exclusively with a polypeptide of 16 kD (p16). Quaternary complexes containing cyclins A or B1 and p21/CDK/PCNA also undergo subunit rearrangement in transformed cells. Both PCNA and p21 are no longer associated with CDC2-cyclin B1 binary complexes. Cyclin A complexes no longer contain p21, and a new 19-kD polypeptide (p19) is found in association with cyclin A. The pattern of subunit rearrangement of cyclin-CDK complexes in SV40-transformed cells is also shared in those containing adeno- or papilloma viral oncoproteins. Rearrangement also occurs in p53-deficient cells derived from Li-Fraumeni patients that carry no known DNA tumor virus. These findings suggest a mechanism by which oncogenic proteins alter the cell cycle of transformed cells.

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Metadata

Authors
Xiong, Y., Zhang, H., & Beach, D.
Venue
Genes & Development
Published
1993-08
Volume
7
Issue
8
Pages
1572-1583
ISSN
  • 0890-9369 (ISSN-L)
  • 1549-5477
OpenAlex
W2076273397
Cited by
507
References
2
Type
posted content
Language
en
Open access
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CoChat. (2026). Citation check: Subunit rearrangement of the cyclin-dependent kinases is associated with cellular transformation. https://app.cochat.ai/papers/10.1101/gad.7.8.1572
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Xiong, Y., Zhang, H., & Beach, D. (1993). Subunit rearrangement of the cyclin-dependent kinases is associated with cellular transformation. Genes & Development. https://doi.org/10.1101/gad.7.8.1572

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