• Register
X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

X

Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.

No
Yes

Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay.

Decapping is a key step in general and regulated mRNA decay. In Saccharomyces cerevisiae it constitutes a rate-limiting step in the nonsense-mediated decay pathway that rids cells of mRNAs containing premature termination codons. Here two human decapping enzymes are identified, hDcp1a and hDcp2, as well as a homolog of hDcp1a, termed hDcp1b. Transiently expressed hDcp1a and hDcp2 proteins localize primarily to the cytoplasm and form a complex in human cell extracts. hDcp1a and hDcp2 copurify with decapping activity, an activity sensitive to mutation of critical hDcp residues. Importantly, coimmunoprecipitation assays demonstrate that hDcp1a and hDcp2 interact with the nonsense-mediated decay factor hUpf1, both in the presence and in the absence of the other hUpf proteins, hUpf2, hUpf3a, and hUpf3b. These data suggest that a human decapping complex may be recruited to mRNAs containing premature termination codons by the hUpf proteins.

Pubmed ID: 12417715

Authors

  • Lykke-Andersen J

Journal

Molecular and cellular biology

Publication Data

December 5, 2002

Associated Grants

None

Mesh Terms

  • Cell Line
  • Endoribonucleases
  • Fungal Proteins
  • Gene Expression Regulation
  • Humans
  • Models, Genetic
  • Molecular Sequence Data
  • Multienzyme Complexes
  • Mutation
  • Protein Biosynthesis
  • RNA Cap-Binding Proteins
  • RNA Helicases
  • RNA, Fungal
  • RNA, Messenger
  • RNA-Binding Proteins
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae Proteins
  • Trans-Activators