PELP1: Structure, biological function and clinical significance

Research output: Contribution to journalReview articlepeer-review

30 Scopus citations


Proline-, glutamic acid-, and leucine-rich protein 1 (PELP1) is a scaffolding protein that functions as a coregulator of several transcription factors and nuclear receptors. Notably, the PELP1 protein has a histone-binding domain, recognizes histone modifications and interacts with several chromatin-modifying complexes. PELP1 serves as a substrate of multitude of kinases, and phosphorylation regulates its functions in various complexes. Further, PELP1 plays essential roles in several pathways including hormonal signaling, cell cycle progression, ribosomal biogenesis, and the DNA damage response. PELP1 expression is upregulated in several cancers, its deregulation contributes to therapy resistance, and it is a prognostic biomarker for breast cancer survival. Recent evidence suggests that PELP1 represents a novel therapeutic target for many hormonal cancers. In this review, we summarized the emerging biological properties and functions of PELP1.

Original languageEnglish (US)
Pages (from-to)128-134
Number of pages7
Issue number1
StatePublished - Jul 1 2016


  • Coregulator
  • Estrogen receptor
  • Hormonal action
  • Nuclear receptor
  • PELP1
  • Signal transduction
  • Transcriptional activation

ASJC Scopus subject areas

  • Genetics


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