Dissection of CDK4-binding and transactivation activities of p34(SEI-1) and comparison between functions of p34(SEI-1) and p16(INK4A)

Biochemistry. 2005 Oct 11;44(40):13246-56. doi: 10.1021/bi0504658.

Abstract

Recent studies showed that p34(SEI-1), also known as TRIP-Br1 or SEI-1, plays a dual role in the regulation of cell-cycle progression. It exhibits the transactivation activity and regulates a number of genes required for G1/S transition, while it also binds and activates cyclin-dependent kinase 4 (CDK4) independent of the inhibitory activity of p16. The goals of this paper are to further dissect the two roles and to compare the functions between SEI-1 and p16. (i) Yeast one-hybrid-based random mutagenesis was first used to identify a number of SEI-1 residues important for LexA-mediated transactivation, including residues L51, K52, L53, H54, L57, and L69 located within the heptad repeat (residues 30-88), a domain required for LexA-mediated transactivation, and two residues M219 and L228 at the C-terminal segment that contributes to transactivation through modulating the heptad repeat. (ii) The functional significance of these residues was further confirmed by site-directed mutagenesis. It was also shown that the heptad repeat-involving transactivation is distinct from the well-known acidic region-involving transactivation. (iii) Yeast two-hybrid-based binding analysis was made possible with the transactivation-negative SEI-1 mutants, and the results showed that some of such mutants retain full ability to bind and activate CDK4. (iv) Site-specific mutants of CDK4 were used to show that there are notable differences among SEI-1, p16, and cyclin D2 in binding to CDK4. (v) The expression levels of SEI-1 and p16 were compared in 32 tumor specimens of human squamous cell carcinomas of the head and neck. The results indicate that SEI-1 was consistently overexpressed, while p16 was consistently underexpressed. These results provide important information on the molecular mechanism of the functions of SEI-1 and on the comparison between SEI-1 and p16 at both molecular and cellular levels.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Carcinoma, Squamous Cell / metabolism
  • Cloning, Molecular
  • Cyclin-Dependent Kinase 4 / metabolism
  • Cyclin-Dependent Kinase 4 / physiology*
  • Cyclin-Dependent Kinase Inhibitor p16 / metabolism*
  • DNA, Complementary / metabolism
  • Dose-Response Relationship, Drug
  • Gene Expression Regulation
  • Head and Neck Neoplasms / metabolism
  • Humans
  • Molecular Sequence Data
  • Mutagenesis
  • Mutagenesis, Site-Directed
  • Mutation
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / metabolism*
  • Polymerase Chain Reaction
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • RNA / chemistry
  • Reverse Transcriptase Polymerase Chain Reaction
  • Structure-Activity Relationship
  • Trans-Activators / chemistry
  • Trans-Activators / metabolism*
  • Transcription Factors
  • Transcriptional Activation*
  • Two-Hybrid System Techniques

Substances

  • Cyclin-Dependent Kinase Inhibitor p16
  • DNA, Complementary
  • Nuclear Proteins
  • SERTAD1 protein, human
  • Trans-Activators
  • Transcription Factors
  • RNA
  • Cyclin-Dependent Kinase 4