Results 21 to 30 of about 3,329 (143)
Using FRET to Study RanGTP Gradients in Live Mouse Oocytes.
, 2012 International audienceOocytes are extremely large cells that have to coordinate accurate chromosome segregation, asymmetric cytoplasm partitioning together with their own development as fertilizable gametes. For this, they undergo both global (cell cycle
Dumont, Julien +3 more
core +3 more sources
CHD4 Is a RanGTP-Dependent MAP that Stabilizes Microtubules and Regulates Bipolar Spindle Formation [PDF]
Current Biology, 2013 peer reviewedBackground Production of the GTP-bound form of the Ran GTPase (RanGTP) around chromosomes induces spindle assembly by activating nuclear localization signal (NLS)-containing proteins.
Krijgsveld, Jeroen +7 more
core +5 more sources
Induced opening of conformational switch I in GTP-bound Ran GTPase. [PDF]
Protein SciAbstract Ran is a small GTPase that regulates nucleocytoplasmic transport by cycling between an inactive GDP‐bound and active GTP‐bound state. Structurally, Ran consists of a globular G‐domain and a C‐terminal region that includes a C‐terminal helix. The switch I and II regions of the G‐domain undergo major conformational changes upon GTP hydrolysis ...
Czigleczki J, Dudas B, Balog E.
europepmc +2 more sources
RanGTP-regulated interactions of CRM1 with nucleoporins and a shuttling DEAD-box helicase [PDF]
Molecular and Cellular Biology, 1999 CRM1 is an export receptor mediating rapid nuclear exit of proteins and RNAs to the cytoplasm. CRM1 export cargoes include proteins with a leucine- rich nuclear export signal (NES) that bind directly to CRM1 in a trimeric complex with RanGTP.
Kjems, Jørgen +10 more
core +3 more sources
Histone Nuclear Import and Beyond: Multifunctional Roles of Importins. [PDF]
BioessaysEfficient nuclear import of histones requires coordinated action between histone chaperones and nuclear import receptors. Importin‐4, Importin‐9, and Importin‐β/7 not only transport specific histone complexes but also act as chaperones, stabilizing histones and ensuring their protected delivery for nucleosome assembly, highlighting importins as central
Bernardes N, Chook YM.
europepmc +2 more sources
Targeting the nuclear export receptor exportin-1 in acute myeloid leukaemia: From biology to clinical translation. [PDF]
Clin Transl Med• XPO1 hyperactivation promotes leukaemogenesis by altering nucleocytoplasmic transport and transcriptional control in acute myeloid leukaemia (AML). • Selinexor and eltanexor show preferential activity in NPM1‐mutated, DEK::NUP214‐positive and SF3B1‐mutated myeloid neoplasms.
Liu Y, Yun X, Ding W, Li S, Liu H.
europepmc +2 more sources
Identification and Characterization of a Novel RanGTP-binding Protein in the Yeast Saccharomyces cerevisiae [PDF]
Journal of Biological Chemistry, 2003 International audienceThe small Ras-like GTPase Ran plays an essential role in the transport of macromolecules in and out of the nucleus and has been implicated in spindle (1,2 ) and nuclear envelope formation (3,4 ) during mitosis in higher eukaryotes ...
Gerstberger, Thomas +6 more
core +4 more sources
XPO5 promotes primary miRNA processing independently of RanGTP [PDF]
Nature Communications, 2020 AbstractXPO5 mediates nuclear export of miRNA precursors in a RanGTP-dependent manner. However, XPO5-associated RNA species have not been determined globally and it is unclear whether XPO5 has any additional functions other than nuclear export. Here we show XPO5 pervasively binds to double-stranded RNA regions found in some clustered primary miRNA ...
Jingjing Wang +6 more
openaire +3 more sources
The RanGTP gradient – a GPS for the mitotic spindle [PDF]
Journal of Cell Science, 2008 The GTPase Ran has a key role in nuclear import and export, mitotic spindle assembly and nuclear envelope formation. The cycling of Ran between its GTP- and GDP-bound forms is catalyzed by the chromatin-bound guanine nucleotide exchange factor RCC1 and the cytoplasmic Ran GTPase-activating protein RanGAP.
Petr, Kalab, Rebecca, Heald
openaire +2 more sources
Mechanism of RanGTP priming H2A-H2B release from Kap114 in an atypical RanGTP•Kap114•H2A-H2B complex
Proceedings of the National Academy of Sciences, 2022 Abstract Previously we showed that the nuclear import receptor Importin-9 wraps around the H2A-H2B core to chaperone and transport it from the cytoplasm to the nucleus. However, unlike most nuclear import systems where RanGTP dissociates cargoes from their importins, RanGTP binds stably to the Importin-9•H2A-H2B complex and formation of
Jenny Jiou +6 more
openaire +2 more sources