Biophysical mechanism of rhomboid proteolysis: Setting a foundation for therapeutics

被引：7

作者：

Bondar, Ana-Nicoleta ^{[1
]}

机构：

[1] Free Univ Berlin, Theoret Mol Biophys Grp, Dept Phys, Arnimallee 14, D-14195 Berlin, Germany

来源：

SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY | 2016年 / 60卷

关键词：

Rhomboid proteases; Reaction coordinate; Lipid/protein interactions; Protein dynamics; Hydrogen bonding; INTRAMEMBRANE PROTEOLYSIS; SUBSTRATE-SPECIFICITY; STRUCTURAL BASIS; FAMILY PROTEASE; GAMMA-SECRETASE; MEMBRANE; DYNAMICS; PROTEINS; REVEALS; SERINE;

D O I：

10.1016/j.semcdb.2016.09.006

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Rhomboid proteolysis is an important cellular process that involves cleavage of transmembrane substrates by membrane-embedded rhomboid proteases. Such proteases can cleave substrates with essential roles in the cell, and their action has been implicated in human diseases. The remarkable sensitivity of rhomboid proteolysis to the lipid membrane environment highlights the usefulness of rhomboid pro teases as model systems to dissect the role of lipids in reaction mechanisms of membrane proteins, including cleavage of substrates by gamma-secretase. I discuss here the hydrogen-bond networks likely important for the reaction mechanism of rhomboid proteases, and how the composition of the lipid membrane can alter protein dynamics. (C) 2016 Elsevier Ltd. All rights reserved.

引用

页码：46 / 51

页数：6

共 64 条

[1] Mammalian EGF receptor activation by the rhomboid protease RHBDL2 [J].

Adrain, Colin ;

Strisovsky, Kvido ;

Zettl, Markus ;

Hu, Landian ;

Lemberg, Marius K. ;

Freeman, Matthew .

EMBO REPORTS, 2011, 12 (05) :421-427

[2] Allosteric regulation of rhomboid intramembrane proteolysis [J].

Arutyunova, Elena ;

Panwar, Pankaj ;

Skiba, Pauline M. ;

Gale, Nicola ;

Mak, Michelle W. ;

Lemieux, M. Joanne .

EMBO JOURNAL, 2014, 33 (17) :1869-1881

[3] Sampling the conformational space of the catalytic subunit of human γ-secretase [J].

Bai, Xiao-chen ;

Rajendra, Eeson ;

Yang, Guanghui ;

Shi, Yigong ;

Scheres, Sjors H. W. .

ELIFE, 2015, 4

[4] An atomic structure of human γ-secretase [J].

Bai, Xiao-chen ;

Yan, Chuangye ;

Yang, Guanghui ;

Lu, Peilong ;

Ma, Dan ;

Sun, Linfeng ;

Zhou, Rui ;

Scheres, Sjors H. W. ;

Shi, Yigong .

NATURE, 2015, 525 (7568) :212-+

[5] Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate [J].

Baker, Rosanna P. ;

Young, Keith ;

Feng, Liang ;

Shi, Yigong ;

Urban, Sinisa .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (20) :8257-8262

[6] Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria [J].

Baker, Rosanna P. ;

Wijetilaka, Ruvini ;

Urban, Sinisa .

PLOS PATHOGENS, 2006, 2 (10) :922-932

[7]

Baker RP, 2012, NAT CHEM BIOL, V8, P759, DOI [10.1038/nchembio.1021, 10.1038/NCHEMBIO.1021]

[8] Structural basis for intramembrane proteolysis by rhomboid serine proteases [J].

Ben-Shem, Adam ;

Fass, Deborah ;

Bibi, Eitan .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (02) :462-466

[9] Key role of electrostatic interactions in bacteriorhodopsin proton transfer [J].

Bondar, AN ;

Fischer, S ;

Smith, JC ;

Elstner, M ;

Suhai, S .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2004, 126 (44) :14668-14677

[10] Structural and energetic determinants of primary proton transfer in bacteriorhodopsin [J].

Bondar, Ana-Nicoleta ;

Smitha, Jeremy C. ;

Fischer, Stefan .

PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES, 2006, 5 (06) :547-552

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