Annexin A4 self-association modulates general membrane protein mobility in living cells

Alen Piljić, Carsten Schultz

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

Annexins are Ca2+-regulated phospholipid-binding proteins whose function is only partially understood. Annexin A4 is a member of this family that is believed to be involved in exocytosis and regulation of epithelial Cl- secretion. In this work, fluorescent protein fusions of annexin A4 were used to investigate Ca2+-induced annexin A4 translocation and self-association on membrane surfaces in living cells. We designed a novel, genetically encoded, FRET sensor (CYNEX4) that allowed for easy quantification of translocation and self-association. Mobility of annexin A4 on membrane surfaces was investigated by FRAP. The experiments revealed the immobile nature of annexin A4 aggregates on membrane surfaces, which in turn strongly reduced the mobility of transmembrane and plasma membrane associated proteins. Our work provides mechanistic insight into how annexin A4 may regulate plasma membrane protein function.

Original languageEnglish (US)
Pages (from-to)3318-3328
Number of pages11
JournalMolecular Biology of the Cell
Volume17
Issue number7
DOIs
StatePublished - Jul 2006
Externally publishedYes

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Annexin A4
Membrane Proteins
Membranes
Blood Proteins
Cell Membrane
Annexins
Exocytosis
Phospholipids
Carrier Proteins

ASJC Scopus subject areas

  • Cell Biology
  • Genetics
  • Molecular Biology

Cite this

Annexin A4 self-association modulates general membrane protein mobility in living cells. / Piljić, Alen; Schultz, Carsten.

In: Molecular Biology of the Cell, Vol. 17, No. 7, 07.2006, p. 3318-3328.

Research output: Contribution to journalArticle

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