Oestrogen-mediated tyrosine phosphorylation of caveolin-1 and its effect on the oestrogen receptor localisation

An in vivo study

A. Kiss, Ágnes Turi, Nándor Müllner, Eniko Kovács, Erzsébet Botos, Anikó Greger

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Recently, it has been shown that 17β estradiol (E2) induces a rapid and transient activation of the Src ERK phosphorylation cascade: a clear indication that the α oestrogen receptor (ERα) is able to associate with the plasma membrane. Increasing evidence suggests that caveolae, which are caveolin-1 containing, highly hydrophobic membrane domains, play an important role in E2 induced signal transduction. Caveolae can accumulate signalling molecules preferentially; thus, they may have a regulatory role in signalling processes. Results from previous experiments have shown that E2 treatment decreased the number of surface connected caveolae significantly in uterine smooth muscle cells and also downregulated the expression of caveolin-1. In addition to providing further evidence that ERα interacts with caveolin/caveolae in uterine smooth muscle cells, this study also shows that the interaction between caveolin-1 and ERα is actually facilitated by E2. One of the signal transduction components found to accumulate in caveolae is Src kinase in an amount that increases simultaneously with increases in the amount of ERα. Upon E2 treatment, Src kinase is tyrosine phosphorylated, which, in turn, stimulates Src kinase to phosphorylate caveolin-1. Phosphorylation of caveolin-1 can drive caveolae to pinch off from the plasma membrane, thereby decreasing the amount of plasma membrane-associated caveolin-1. This loss of caveolin/caveolae activates the signal cascade that triggers cell proliferation.

Original languageEnglish
Pages (from-to)128-137
Number of pages10
JournalMolecular and Cellular Endocrinology
Volume245
Issue number1-2
DOIs
Publication statusPublished - Dec 21 2006

Fingerprint

Caveolin 1
Caveolae
Phosphorylation
Estrogen Receptors
Tyrosine
Estrogens
src-Family Kinases
Cell membranes
Caveolins
Signal transduction
Myometrium
Cell Membrane
Muscle
Smooth Muscle Myocytes
Cells
Signal Transduction
Cell proliferation
Estradiol
Chemical activation
Down-Regulation

Keywords

  • ERα-caveolin-1 interaction
  • ICI 182 780
  • Oestrogen
  • Src kinase
  • Tyrosine- phosphorylation

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

Cite this

Oestrogen-mediated tyrosine phosphorylation of caveolin-1 and its effect on the oestrogen receptor localisation : An in vivo study. / Kiss, A.; Turi, Ágnes; Müllner, Nándor; Kovács, Eniko; Botos, Erzsébet; Greger, Anikó.

In: Molecular and Cellular Endocrinology, Vol. 245, No. 1-2, 21.12.2006, p. 128-137.

Research output: Contribution to journalArticle

Kiss, A. ; Turi, Ágnes ; Müllner, Nándor ; Kovács, Eniko ; Botos, Erzsébet ; Greger, Anikó. / Oestrogen-mediated tyrosine phosphorylation of caveolin-1 and its effect on the oestrogen receptor localisation : An in vivo study. In: Molecular and Cellular Endocrinology. 2006 ; Vol. 245, No. 1-2. pp. 128-137.
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