Results 81 to 90 of about 7,148,227 (413)

Localization-Dependent and -Independent Roles of SLX4 in Regulating Telomeres

Cell Reports, 2013
SLX4, a scaffold for structure-specific DNA repair nucleases, is important for several types of DNA repair. Many repair proteins bind to sites of DNA damage, resulting in subnuclear “foci,” but SLX4 forms foci in human cells even without DNA damage ...
Jamie S.J. Wilson, Agueda M. Tejera, Dennis Castor, Rachel Toth, Maria A. Blasco, John Rouse   +5 more
doaj   +1 more source

A conserved phosphorylation site regulates the transcriptional function of ETHYLENE-INSENSITIVE3-like1 in tomato [PDF]

, 2011
ETHYLENE-INSENSITIVE3/ETHYLENE-INSENSITIVE3-like (EIN3/EIL) transcription factors are important downstream components of the ethylene transduction pathway known to regulate the transcription of early ethylene-responsive genes in plants.
Abel, Alonso, Chang, Chao, Fan, Fryer, Gerber, Girod, Guo, Hellens, J. Li, Kammann, Kieber, Kim, Klimczak, Kosugi, L. Tang, Lehman, M. Bouzayen, M. Zouine, Mishra, Montgomery, Raz, Riechmann, Riechmann, Shaner, Sharma, Solano, Stepanova, Tieman, Y. Yang, Yamamoto, Yamasaki, Yokotani, Yoo, Z. Li, Zhou, Zhuang   +37 more
core   +2 more sources

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

FEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes, Guilherme M. Azevedo, Amanda P. Barcellos, Diana Bahia   +3 more
wiley   +1 more source

Cascades of multisite phosphorylation control Sic1 destruction at the onset of S phase. [PDF]

, 2011
Multisite phosphorylation of proteins has been proposed to transform a graded protein kinase signal into an ultrasensitive switch-like response. Although many multiphosphorylated targets have been identified, the dynamics and sequence of individual ...
Balog, Eva Rose M, Iofik, Anna, Kõivomägi, Mardo, Lepiku, Martin, Loog, Mart, Morgan, David O, Rubin, Seth M, Valk, Ervin, Venta, Rainis   +8 more
core   +2 more sources

Interplay between circadian and other transcription factors—Implications for cycling transcriptome reprogramming

FEBS Letters, EarlyView.
This perspective highlights emerging insights into how the circadian transcription factor CLOCK:BMAL1 regulates chromatin architecture, cooperates with other transcription factors, and coordinates enhancer dynamics. We propose an updated framework for how circadian transcription factors operate within dynamic and multifactorial chromatin landscapes ...
Xinyu Y. Nie, Jerome S. Menet
wiley   +1 more source

Disordered but rhythmic—the role of intrinsic protein disorder in eukaryotic circadian timing

FEBS Letters, EarlyView.
Unstructured domains known as intrinsically disordered regions (IDRs) are present in nearly every part of the eukaryotic core circadian oscillator. IDRs enable many diverse inter‐ and intramolecular interactions that support clock function. IDR conformations are highly tunable by post‐translational modifications and environmental conditions, which ...
Emery T. Usher, Jacqueline F. Pelham
wiley   +1 more source

HMMR/RHAMM recruits SACK1D/FAM83D-CK1α complex at the mitotic spindle to control spindle alignment

iScience
Summary: The SACK1D/FAM83D-CK1α complex assembles at the mitotic spindle to orchestrate proper spindle positioning and error-free progression through mitosis.
Tyrell N. Cartwright, Naveen K. Nakarakanti, Karen Dunbar, Luke J. Fulcher, Selina Bader, Nicola T. Wood, Thomas J. Macartney, Gopal P. Sapkota   +7 more
doaj   +1 more source

Phosphorylation of Spinophilin Modulates Its Interaction with Actin Filaments [PDF]

, 2003
Spinophilin is a protein phosphatase 1 (PP1)- and actin-binding protein that modulates excitatory synaptic transmission and dendritic spine morphology. We report that spinophilin is phosphorylated in vitro by protein kinase A (PKA).
Allen, Patrick B., Benfenati, Fabio, Greengard, Paul, Hsieh-Wilson, Linda C., Nairn, Angus C., Snyder, Gretchen L.   +5 more
core  

Charge environments around phosphorylation sites in proteins [PDF]

, 2008
Background: Phosphorylation is a central feature in many biological processes. Structural analyses have identified the importance of charge-charge interactions, for example mediating phosphorylation-driven allosteric change and protein binding to ...
Kitchen, James, Saunders, Rebecca E., Warwicker, Jim   +2 more
core   +2 more sources

Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation

FEBS Letters, EarlyView.
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe, Tanmay Kumar Mohanty, Rashna Bhandari, Dorothea Fiedler   +3 more
wiley   +1 more source