On the roles of intrinsically disordered proteins and regions in cell communication and signaling

被引:65
作者
Bondos, Sarah E. [1 ]
Dunker, A. Keith [2 ]
Uversky, Vladimir N. [3 ,4 ,5 ]
机构
[1] Texas A&M Hlth Sci Ctr, Dept Mol & Cellular Med, College Stn, TX 77843 USA
[2] Indiana Univ Sch Med, Dept Biochem & Mol Biol, Ctr Computat Biol & Bioinformat, Indianapolis, IN 46202 USA
[3] Univ S Florida, Morsani Coll Med, Dept Mol Med, Tampa, FL 33620 USA
[4] Univ S Florida, Morsani Coll Med, USF Hlth Byrd Alzheimers Res Inst, Tampa, FL 33620 USA
[5] Russian Acad Sci, Pushchino Sci Ctr Biol Res, Fed Res Ctr, Inst Biol Instrumentat, Pushchino, Russia
关键词
Amino acid sequence; Protein structure; Disorder prediction; Intrinsically disordered proteins; NATIVELY UNFOLDED PROTEINS; FUNCTIONAL ANTHOLOGY; DATABASE; DOMAINS; DISPROT; PREDICTION; WAITS;
D O I
10.1186/s12964-021-00774-3
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
For proteins, the sequence -> structure -> function paradigm applies primarily to enzymes, transmembrane proteins, and signaling domains. This paradigm is not universal, but rather, in addition to structured proteins, intrinsically disordered proteins and regions (IDPs and IDRs) also carry out crucial biological functions. For these proteins, the sequence -> IDP/IDR ensemble -> function paradigm applies primarily to signaling and regulatory proteins and regions. Often, in order to carry out function, IDPs or IDRs cooperatively interact, either intra- or inter-molecularly, with structured proteins or other IDPs or intermolecularly with nucleic acids. In this IDP/IDR thematic collection published in Cell Communication and Signaling, thirteen articles are presented that describe IDP/IDR signaling molecules from a variety of organisms from humans to fruit flies and tardigrades ("water bears") and that describe how these proteins and regions contribute to the function and regulation of cell signaling. Collectively, these papers exhibit the diverse roles of disorder in responding to a wide range of signals as to orchestrate an array of organismal processes. They also show that disorder contributes to signaling in a broad spectrum of species, ranging from micro-organisms to plants and animals.
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页数:9
相关论文
共 76 条
[1]   The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins [J].
Appadurai, Rajeswari ;
Uversky, Vladimir N. ;
Srivastava, Anand .
JOURNAL OF MEMBRANE BIOLOGY, 2019, 252 (4-5) :273-292
[2]   The Protein Data Bank [J].
Berman, HM ;
Westbrook, J ;
Feng, Z ;
Gilliland, G ;
Bhat, TN ;
Weissig, H ;
Shindyalov, IN ;
Bourne, PE .
NUCLEIC ACIDS RESEARCH, 2000, 28 (01) :235-242
[3]  
Berman HM., 2002, BIOL CRYSTALLOGR, V58, DOI [10.1107/S09074449020034511:CAS:528:DC%2BD38XktVKhtLg%3D, DOI 10.1107/S09074449020034511:CAS:528:DC%2BD38XKTVKHTLG%3D]
[4]  
Bondos SE, CELL COMMUN SIGNAL, V2021, P19
[5]   Intrinsic Disorder in Transmembrane Proteins: Roles in Signaling and Topology Prediction [J].
Burgi, Jerome ;
Xue, Bin ;
Uversky, Vladimir N. ;
van der Goot, F. Gisou .
PLOS ONE, 2016, 11 (07)
[6]   Structuring the universe of proteins [J].
Burley, SK ;
Bonanno, JB .
ANNUAL REVIEW OF GENOMICS AND HUMAN GENETICS, 2002, 3 :243-262
[7]   Calcineurin [J].
Creamer, Trevor P. .
CELL COMMUNICATION AND SIGNALING, 2020, 18 (01)
[8]   Attributes of short linear motifs [J].
Davey, Norman E. ;
Van Roey, Kim ;
Weatheritt, Robert J. ;
Toedt, Grischa ;
Uyar, Bora ;
Altenberg, Brigitte ;
Budd, Aidan ;
Diella, Francesca ;
Dinkel, Holger ;
Gibson, Toby J. .
MOLECULAR BIOSYSTEMS, 2012, 8 (01) :268-281
[9]   Prevalence of intrinsic disorder in the intracellular region of human single-pass type I proteins: The case of the Notch ligand Delta-4 [J].
De Biasio, Alfredo ;
Guarnaccia, Corrado ;
Popovic, Matija ;
Uversky, Vladimir N. ;
Pintar, Alessandro ;
Pongor, Sandor .
JOURNAL OF PROTEOME RESEARCH, 2008, 7 (06) :2496-2506
[10]   Not an exception to the rule: the functional significance of intrinsically disordered protein regions in enzymes [J].
DeForte, Shelly ;
Uversky, Vladimir N. .
MOLECULAR BIOSYSTEMS, 2017, 13 (03) :463-469