Role of intrinsic disorder in transient interactions of hub proteins

2006 ◽  
Vol 66 (4) ◽  
pp. 761-765 ◽  
Author(s):  
Gajinder Pal Singh ◽  
Mythily Ganapathi ◽  
Debasis Dash
Keyword(s):  
Intrinsic Disorder ◽  
Transient Interactions ◽  
Hub Proteins

scholarly journals Role of Intrinsic Disorder in Animal Desiccation Tolerance

PROTEOMICS ◽  
2018 ◽  
Vol 18 (21-22) ◽  
pp. 1800067 ◽  
Author(s):  
Brett Janis ◽  
Clinton Belott ◽  
Michael A. Menze
Keyword(s):  
Desiccation Tolerance ◽  
Intrinsic Disorder

scholarly journals Intrinsic Disorder Is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes

2006 ◽  
Vol 2 (8) ◽  
pp. e100 ◽  
Author(s):  
Chad Haynes ◽  
Christopher J Oldfield ◽  
Fei Ji ◽  
Niels Klitgord ◽  
Michael E Cusick ◽  
...  
Keyword(s):  
Intrinsic Disorder ◽  
Hub Proteins

scholarly journals The Interaction between Sgt1p and Skp1p Is Regulated by HSP90 Chaperones and Is Required for Proper CBF3 Assembly

2004 ◽  
Vol 24 (20) ◽  
pp. 8938-8950 ◽  
Author(s):  
Linda B. Lingelbach ◽  
Kenneth B. Kaplan
Keyword(s):  
Chromosome Segregation ◽  
Protein Complexes ◽  
Dependent Manner ◽  
Carboxy Terminus ◽  
Genetic Studies ◽  
Cellular Processes ◽  
Transient Interactions ◽  
Precise Relationship ◽  
Protein Complex Assembly

ABSTRACT Sgt1p is a well-conserved protein proposed to be involved in a number of cellular processes. Genetic studies of budding yeast suggest a role for SGT1 in signal transduction, cell cycle advance, and chromosome segregation. Recent evidence has linked Sgt1p to HSP90 chaperones, although the precise relationship between these proteins is unclear. To further explore the role of Sgt1p in these processes, we have characterized the interactions among Sgt1p, the inner kinetochore complex CBF3, and HSP90 chaperones. We show that the amino terminus of Sgt1p interacts with CBF3 subunits Skp1p and Ctf13p. HSP90 interacts with Sgt1p and, in combination with the carboxy terminus of Sgt1p, regulates the interaction between Sgt1p and Skp1p in a nucleotide-dependent manner. While the Sgt1p-Skp1p interaction is required for CBF3 assembly, mutations that stabilize this interaction prevent the turnover of protein complexes important for CBF3 assembly. We propose that HSP90 and Sgt1p act together as a molecular switch, maintaining transient interactions required to balance protein complex assembly with turnover.

HMGN dynamics and chromatin function

2003 ◽  
Vol 81 (3) ◽  
pp. 113-122 ◽  
Author(s):  
Frédéric Catez ◽  
Jae-Hwan Lim ◽  
Robert Hock ◽  
Yuri V Postnikov ◽  
Michael Bustin
Keyword(s):  
Binding Sites ◽  
Protein Composition ◽  
Nuclear Proteins ◽  
Chromatin Interactions ◽  
Binding Partners ◽  
Nucleosomal Dna ◽  
Transient Interactions ◽  
And Function ◽  
Nucleosome Binding

Recent studies indicate that most nuclear proteins, including histone H1 and HMG are highly mobile and their interaction with chromatin is transient. These findings suggest that the structure of chromatin is dynamic and the protein composition at any particular chromatin site is not fixed. Here we discuss how the dynamic behavior of the nucleosome binding HMGN proteins affects the structure and function of chromatin. The high intranuclear mobility of HMGN insures adequate supply of protein throughout the nucleus and serves to target these proteins to their binding sites. Transient interactions of the proteins with nucleosomes destabilize the higher order chromatin, enhance the access to nucleosomal DNA, and impart flexibility to the chromatin fiber. While roaming the nucleus, the HMGN proteins encounter binding partners and form metastable multiprotein complexes, which modulate their chromatin interactions. Studies with HMGN proteins underscore the important role of protein dynamics in chromatin function.Key words: HMG, nuclear proteins, chromatin, HMGN.

scholarly journals Relationships between Subcellular Localization, Hub Proteins and Intrinsic Disorder

2017 ◽  
Vol 57 (2) ◽  
pp. 085-089
Author(s):  
Motonori OTA ◽  
Satoshi FUKUCHI ◽  
Ryotaro KOIKE
Keyword(s):  
Subcellular Localization ◽  
Intrinsic Disorder ◽  
Hub Proteins

scholarly journals Seeing β-arrestin in action: The role of β-arrestins in Histamine 1 Receptor signaling

2019 ◽  
Author(s):  
A Pietraszewska-Bogiel ◽  
J Goedhart
Keyword(s):  
G Protein ◽  
Live Cell ◽  
Chemical Mediator ◽  
Intracellular Location ◽  
Erk Activation ◽  
Class A ◽  
Transient Interactions ◽  
Major Chemical ◽  
G Protein Coupled

ABSTRACTß-arrestins regulate G protein-coupled receptor functions by influencing their signaling activity and intracellular location. Histamine is a major chemical mediator of allergic reactions, and its action is mainly mediated by the Gq/11- and Gi-coupled H1R. Contrary to accumulating insights into G protein-mediated signaling downstream of H1R, very little is known about the function of ß-arrestins in H1R signaling. Here, we describe dynamic, live cell measurements of ß-arrestin recruitment upon H1R activation in HEK293TN cells. Our observations classify H1R as a class A receptor, undergoing transient interactions with ß-arrestin. To investigate the relative contributions of G proteins and ß-arrestins to H1R signaling, we use specific G protein inhibitors, as well as ß-arrestin overexpression and depletion, and quantify various signaling outcomes in a panel of dynamic, live cell biosensor assays. Overall, we link ß-arrestins to desensitization of H1R-mediated signaling and show that ERK activation downstream of endogenous (HeLa, HUVEC) or transiently expressed (HEK293TN) H1R is largely Gq-mediated.

scholarly journals Multivalency regulates activity in an intrinsically disordered transcription factor

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Sarah Clark ◽  
Janette B Myers ◽  
Ashleigh King ◽  
Radovan Fiala ◽  
Jiri Novacek ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Transcriptional Activity ◽  
Target Gene ◽  
Intrinsic Disorder ◽  
Negative Cooperativity ◽  
Intrinsically Disordered ◽  
Main Target ◽  
Recognition Motifs ◽  
Cellular Transcription

The transcription factor ASCIZ (ATMIN, ZNF822) has an unusually high number of recognition motifs for the product of its main target gene, the hub protein LC8 (DYNLL1). Using a combination of biophysical methods, structural analysis by NMR and electron microscopy, and cellular transcription assays, we developed a model that proposes a concerted role of intrinsic disorder and multiple LC8 binding events in regulating LC8 transcription. We demonstrate that the long intrinsically disordered C-terminal domain of ASCIZ binds LC8 to form a dynamic ensemble of complexes with a gradient of transcriptional activity that is inversely proportional to LC8 occupancy. The preference for low occupancy complexes at saturating LC8 concentrations with both human and Drosophila ASCIZ indicates that negative cooperativity is an important feature of ASCIZ-LC8 interactions. The prevalence of intrinsic disorder and multivalency among transcription factors suggests that formation of heterogeneous, dynamic complexes is a widespread mechanism for tuning transcriptional regulation.

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