Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains

Robert Stahelin, Fei Long, Brian J. Peter, Diana Murray, Pietro De Camilli, Harvey T. McMahon, Wonhwa Cho

Research output: Contribution to journalArticle

133 Citations (Scopus)

Abstract

Epsin and AP180/CALM are endocytotic accessory proteins that have been implicated in the formation of clathrin-coated pits. Both proteins have phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2)-binding domains in their N termini, but these domains are structurally and functionally different. To understand the basis of their distinct properties, we measured the PtdIns(4,5)P2-dependent membrane binding of the epsin N-terminal homology (ENTH) domain and the AP180 N-terminal homology (ANTH) domain by means of surface plasmon resonance and monolayer penetration techniques and also calculated the effect of PtdIns(4,5)P2 on the electrostatic potential of these domains. PtdIns(4,5)P2 enhances the electrostatic membrane association of both domains; however, PtdIns(4,5)P2 binding exerts distinct effects on their membrane dissociation. Specifically, PtdIns(4,5)P2 induces the membrane penetration of the N-terminal α-helix of the ENTH domain, which slows the membrane dissociation of the domain and triggers the membrane deformation. These results provide the biophysical explanation for the membrane bending activity of epsin and its ENTH domain.

Original languageEnglish (US)
Pages (from-to)28993-28999
Number of pages7
JournalJournal of Biological Chemistry
Volume278
Issue number31
DOIs
StatePublished - Aug 1 2003
Externally publishedYes

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Phosphatidylinositol 4,5-Diphosphate
Membranes
Static Electricity
Electrostatics
Clathrin
Surface Plasmon Resonance
Accessories
Surface plasmon resonance
Phosphatidylinositols
epsin
Monolayers
Proteins
Association reactions

ASJC Scopus subject areas

  • Biochemistry

Cite this

Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains. / Stahelin, Robert; Long, Fei; Peter, Brian J.; Murray, Diana; De Camilli, Pietro; McMahon, Harvey T.; Cho, Wonhwa.

In: Journal of Biological Chemistry, Vol. 278, No. 31, 01.08.2003, p. 28993-28999.

Research output: Contribution to journalArticle

Stahelin, Robert ; Long, Fei ; Peter, Brian J. ; Murray, Diana ; De Camilli, Pietro ; McMahon, Harvey T. ; Cho, Wonhwa. / Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains. In: Journal of Biological Chemistry. 2003 ; Vol. 278, No. 31. pp. 28993-28999.
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