Results 41 to 50 of about 97,972 (258)

Protein sub-nuclear localization prediction using SVM and Pfam domain information. [PDF]

PLoS ONE, 2014
The nucleus is the largest and the highly organized organelle of eukaryotic cells. Within nucleus exist a number of pseudo-compartments, which are not separated by any membrane, yet each of them contains only a specific set of proteins.
Ravindra Kumar, Sohni Jain, Bandana Kumari, Manish Kumar   +3 more
doaj   +1 more source

Spatiotemporal and quantitative analyses of phosphoinositides – fluorescent probe—and mass spectrometry‐based approaches

FEBS Letters, EarlyView.
Fluorescent probes allow dynamic visualization of phosphoinositides in living cells (left), whereas mass spectrometry provides high‐sensitivity, isomer‐resolved quantitation (right). Their synergistic use captures complementary aspects of lipid signaling. This review illustrates how these approaches reveal the spatiotemporal regulation and quantitative
Hiroaki Kajiho, Shin Morioka, Junko Sasaki, Takehiko Sasaki   +3 more
wiley   +1 more source

Detailed characterisation of the trypanosome nuclear pore architecture reveals conserved asymmetrical functional hubs that drive mRNA export.

PLoS Biology
Nuclear export of mRNAs requires loading the mRNP to the transporter Mex67/Mtr2 in the nucleoplasm, controlled access to the pore by the basket-localised TREX-2 complex and mRNA release at the cytoplasmic site by the DEAD-box RNA helicase Dbp5 ...
Bernardo Papini Gabiatti, Johanna Krenzer, Silke Braune, Timothy Krüger, Martin Zoltner, Susanne Kramer   +5 more
doaj   +1 more source

The nuclear envelope protein TMEM209 is an integral component of the nuclear pore complex and interacts with Nup210. [PDF]

J Cell Sci
ABSTRACT A highly curved membrane region connecting the inner and the outer nuclear membrane serves as a platform where nucleoporins with one or more transmembrane domains promote anchoring of the nuclear pore complex to the nuclear envelope.
Kohlhause D, Spillner C, Alcalde Zapata V, Lenz C, Urlaub H, Kohl T, Lehnart SE, Gerace L, Kehlenbach RH.   +8 more
europepmc   +6 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

Spatial structure of disordered proteins dictates conductance and selectivity in nuclear pore complex mimics

eLife, 2018
Nuclear pore complexes (NPCs) lined with intrinsically disordered FG-domains act as selective gatekeepers for molecular transport between the nucleus and the cytoplasm in eukaryotic cells.
Adithya N Ananth, Ankur Mishra, Steffen Frey, Arvind Dwarkasing, Roderick Versloot, Erik van der Giessen, Dirk Görlich, Patrick Onck, Cees Dekker   +8 more
doaj   +1 more source

An upstream open reading frame regulates expression of the mitochondrial protein Slm35 and mitophagy flux

FEBS Letters, EarlyView.
This study reveals how the mitochondrial protein Slm35 is regulated in Saccharomyces cerevisiae. The authors identify stress‐responsive DNA elements and two upstream open reading frames (uORFs) in the 5′ untranslated region of SLM35. One uORF restricts translation, and its mutation increases Slm35 protein levels and mitophagy.
Hernán Romo‐Casanueva, Ariann E. Mendoza‐Martínez, P. Abril Medina‐Flores, Carlos Campero‐Basaldua, Alexander DeLuna, Soledad Funes   +5 more
wiley   +1 more source

Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import [PDF]

FEBS Letters, 2001
The trafficking of macromolecules between cytoplasm and nucleus through nuclear pore complexes is mediated by specific carrier molecules such as members of the importin‐β family. Nuclear pore proteins (nucleoporins) frequently contain sequence repeats based on FG cores and carriers appear to move their cargo through the pores by hopping between ...
Stewart, M, Baker, RP, Bayliss, R, Clayton, L, Grant, RP, Littlewood, T, Matsuura, Y   +6 more
openaire   +3 more sources

Desmin’s conformational modulation by hydrophobicity

Türk Biyokimya Dergisi
Nucleocytoplasmic transport is one of the key features in regulation of cellular physiology. Developing a better understanding of the molecular mechanism underlying the nucleocytoplasmic shuttling of proteins can broaden our perspective and understanding
Kural Mangıt Ecem, Cevheroğlu Orkun, Dinçer Pervin   +2 more
doaj   +1 more source

Torsin ATPases: Harnessing Dynamic Instability for Function

Frontiers in Molecular Biosciences, 2017
Torsins are essential, disease-relevant AAA+ (ATPases associated with various cellular activities) proteins residing in the endoplasmic reticulum and perinuclear space, where they are implicated in a variety of cellular functions.
Anna R. Chase, Ethan Laudermilch, Christian Schlieker, Christian Schlieker   +3 more
doaj   +1 more source