Transmembrane helix heterodimerization in lipid bilayers: Probing the energetics behind autosomal dominant growth disorders

Mikhail Merzlyakov; Min You; Edwin Li; Kalina Hristova

doi:10.1016/j.jmb.2006.01.086

Transmembrane helix heterodimerization in lipid bilayers: Probing the energetics behind autosomal dominant growth disorders

Mikhail Merzlyakov, Min You, Edwin Li, Kalina Hristova

Whiting School of Engineering

Research output: Contribution to journal › Article › peer-review

34 Scopus citations

Abstract

Here, we show that the energetics of transmembrane helix heterodimer formation can be characterized in liposomes using Förster resonance energy transfer (FRET). We present the theory and the protocol for measuring the free energy of heterodimerization, and the total (hetero and homo-dimeric) dimer fraction. We use the presented methodology to determine the propensity for heterodimer formation between wild-type fibroblast growth factor receptor 3 (FGFR3) transmembrane domain and the Ala391Glu mutant, linked to Crouzon syndrome with acanthosis nigricans.

Original language	English (US)
Pages (from-to)	1-7
Number of pages	7
Journal	Journal of molecular biology
Volume	358
Issue number	1
DOIs	https://doi.org/10.1016/j.jmb.2006.01.086
State	Published - Apr 21 2006

Keywords

FRET
Fibroblast growth factor receptor 3
Heterodimer
Receptor tyrosine kinase
Transmembrane domain

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/j.jmb.2006.01.086

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title = "Transmembrane helix heterodimerization in lipid bilayers: Probing the energetics behind autosomal dominant growth disorders",

abstract = "Here, we show that the energetics of transmembrane helix heterodimer formation can be characterized in liposomes using F{\"o}rster resonance energy transfer (FRET). We present the theory and the protocol for measuring the free energy of heterodimerization, and the total (hetero and homo-dimeric) dimer fraction. We use the presented methodology to determine the propensity for heterodimer formation between wild-type fibroblast growth factor receptor 3 (FGFR3) transmembrane domain and the Ala391Glu mutant, linked to Crouzon syndrome with acanthosis nigricans.",

keywords = "FRET, Fibroblast growth factor receptor 3, Heterodimer, Receptor tyrosine kinase, Transmembrane domain",

author = "Mikhail Merzlyakov and Min You and Edwin Li and Kalina Hristova",

note = "Funding Information: We thank Xue Han for technical assistance and Dr W. C. Wimley for reading the manuscript prior to publication. This work was supported by Research Scholar Grant RSG-04-201-01 from the American Cancer Society (to K.H.) and, in part, by NSF MCB-0315663 (to K.H.).",

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doi = "10.1016/j.jmb.2006.01.086",

language = "English (US)",

volume = "358",

pages = "1--7",

journal = "Journal of Molecular Biology",

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T1 - Transmembrane helix heterodimerization in lipid bilayers

T2 - Probing the energetics behind autosomal dominant growth disorders

AU - Merzlyakov, Mikhail

AU - You, Min

AU - Li, Edwin

AU - Hristova, Kalina

N1 - Funding Information: We thank Xue Han for technical assistance and Dr W. C. Wimley for reading the manuscript prior to publication. This work was supported by Research Scholar Grant RSG-04-201-01 from the American Cancer Society (to K.H.) and, in part, by NSF MCB-0315663 (to K.H.).

PY - 2006/4/21

Y1 - 2006/4/21

N2 - Here, we show that the energetics of transmembrane helix heterodimer formation can be characterized in liposomes using Förster resonance energy transfer (FRET). We present the theory and the protocol for measuring the free energy of heterodimerization, and the total (hetero and homo-dimeric) dimer fraction. We use the presented methodology to determine the propensity for heterodimer formation between wild-type fibroblast growth factor receptor 3 (FGFR3) transmembrane domain and the Ala391Glu mutant, linked to Crouzon syndrome with acanthosis nigricans.

AB - Here, we show that the energetics of transmembrane helix heterodimer formation can be characterized in liposomes using Förster resonance energy transfer (FRET). We present the theory and the protocol for measuring the free energy of heterodimerization, and the total (hetero and homo-dimeric) dimer fraction. We use the presented methodology to determine the propensity for heterodimer formation between wild-type fibroblast growth factor receptor 3 (FGFR3) transmembrane domain and the Ala391Glu mutant, linked to Crouzon syndrome with acanthosis nigricans.

KW - FRET

KW - Fibroblast growth factor receptor 3

KW - Heterodimer

KW - Receptor tyrosine kinase

KW - Transmembrane domain

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DO - 10.1016/j.jmb.2006.01.086

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JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

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Transmembrane helix heterodimerization in lipid bilayers: Probing the energetics behind autosomal dominant growth disorders

Abstract

Keywords

ASJC Scopus subject areas

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