GAS, a new glutamate-rich protein, interacts differentially with SRCs and is involved in oestrogen receptor function

EMBO Rep. 2009 Jan;10(1):51-7. doi: 10.1038/embor.2008.223. Epub 2008 Nov 28.

Abstract

Steroid receptor coactivators (SRCs) exert profound effects on animal development and physiology. Genetic ablation experiments indicate that various SRC proteins might have differential physiological roles; however, clear evidence of functional specificity has not yet been shown at the molecular level. Here we report the identification of a new SRC1 interacting protein, glutamate-rich coactivator interacting with SRC1 (GAS), which contains a central glutamate-rich region and has transactivation activity. Interestingly, GAS interacts only with SRC1, and not with glucocorticoid receptor interacting protein 1 (GRIP1) or amplified in breast cancer 1 (AIB1), the other two members of the SRC family. It interacts with oestrogen receptor-alpha (ERalpha) and participates in both oestrogen receptor-regulated gene transcription and oestrogen-stimulated G1/S cell-cycle transition. Our data thus indicate that GAS is a new transcription cofactor and that different SRCs are associated with distinct secondary cofactors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cell Cycle Proteins
  • Cell Line
  • Cloning, Molecular
  • DNA-Binding Proteins
  • Estrogen Receptor alpha / metabolism*
  • Glutamic Acid / metabolism
  • Humans
  • Molecular Sequence Data
  • Nuclear Proteins
  • Organ Specificity
  • Protein Binding
  • Receptors, Steroid / metabolism*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Transcriptional Activation / genetics

Substances

  • Carrier Proteins
  • Cell Cycle Proteins
  • DNA-Binding Proteins
  • Estrogen Receptor alpha
  • Nuclear Proteins
  • PAGR1 protein, human
  • Receptors, Steroid
  • Glutamic Acid