The Mechanisms of HAMP-Mediated Signaling in Transmembrane Receptors

被引：80

作者：

Ferris, Hedda U. ^{[1
]}

Dunin-Horkawicz, Stanislaw ^{[1
]}

Mondejar, Laura Garcia ^{[2
]}

Hulko, Michael ^{[1
]}

Hantke, Klaus ^{[2
]}

Martin, Joerg ^{[1
]}

Schultz, Joachim E. ^{[2
]}

Zeth, Kornelius ^{[1
]}

Lupas, Andrei N. ^{[1
]}

Coles, Murray ^{[1
]}

机构：

[1] Max Planck Inst Dev Biol, Dept Prot Evolut, D-72076 Tubingen, Germany

[2] Univ Tubingen, Sch Pharm, Dept Pharmaceut Biochem, D-72076 Tubingen, Germany

来源：

STRUCTURE | 2011年 / 19卷 / 03期

关键词：

ESCHERICHIA-COLI; DOMAIN; PROTEIN; CHEMORECEPTORS; TRANSDUCTION; ASPARTATE; PROGRAM; KINASE; LINKER; ENVZ;

D O I：

10.1016/j.str.2011.01.006

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

HAMP domains mediate signal transduction in over 7500 enzyme-coupled receptors represented in all kingdoms of life. The HAMP domain of the putative archaeal receptor Af1503 has a parallel, dimeric, four-helical coiled coil structure, but with unusual core packing, related to canonical packing by concerted axial rotation of the helices. This has led to the gearbox model for signal transduction, whereby the alternate packing modes correspond to signaling states. Here we present structures of a series of Af1503 HAMP variants. We show that substitution of a conserved small side chain within the domain core (A291) for larger residues induces a gradual transition in packing mode, involving both changes in helix rotation and bundle shape, which are most prominent at the C-terminal, output end of the domain. These are correlated with activity and ligand response in vitro and in vivo by incorporating Af1503 HAMP into mycobacterial adenylyl cyclase assay systems.

引用

页码：378 / 385

页数：8

共 50 条

[1] Molecular Mechanisms of G Protein-Independent Signaling Mediated by 7-Transmembrane Receptors
Fisyunov, A. I.
NEUROPHYSIOLOGY, 2012, 44 (03) : 255 - 264
[2] Molecular Mechanisms of G Protein-Independent Signaling Mediated by 7-Transmembrane Receptors
А. I. Fisyunov
Neurophysiology, 2012, 44 : 255 - 264
[3] The HAMP domain structure implies helix rotation in transmembrane signaling
Hulko, Michael
Berndt, Franziska
Gruber, Markus
Linder, Juergen U.
Truffault, Vincent
Schultz, Anita
Martin, Joerg
Schultz, Joachim E.
Lupas, Andrei N.
Coles, Murray
CELL, 2006, 126 (05) : 929 - 940
[4] RECEPTORS AND TRANSMEMBRANE SIGNALING
STODDARD, BL
BIEMANN, HP
KOSHLAND, DE
COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY, 1992, 57 : 1 - 15
[5] Signaling Mechanisms of HAMP Domains in Chemoreceptors and Sensor Kinases
Parkinson, John S.
ANNUAL REVIEW OF MICROBIOLOGY, VOL 64, 2010, 2010, 64 : 101 - 122
[6] The HAMP linker in histidine kinase dimeric receptors is critical for symmetric transmembrane signal transduction
Zhu, Y
Inouye, M
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (46) : 48152 - 48158
[7] DIFFERENT TRANSMEMBRANE SIGNALING MECHANISMS MEDIATED BY BAND-3 AND GLYCOPHORIN-A
CHASIS, JA
MCGEE, S
ANSTEE, D
MOHANDAS, N
BLOOD, 1993, 82 (10) : A174 - A174
[8] ER-mediated control for abundance, quality, and signaling of transmembrane immune receptors in plants
Tintor, Nico
Saijo, Yusuke
FRONTIERS IN PLANT SCIENCE, 2014, 5
[9] TRANSMEMBRANE SIGNALING MECHANISMS IN THE ACTION OF INSULIN
CZECH, MP
MASSAGUE, J
PILCH, PF
BEACHY, J
SEALS, JR
EUROPEAN JOURNAL OF CELL BIOLOGY, 1980, 22 (01) : 256 - 256
[10] TRANSMEMBRANE SIGNALING BY LYMPHOCYTE-B RECEPTORS
KLAUS, GGB
IMMUNOLOGY, 1988, : 35 - 37

← 1 2 3 4 5 →