Results 51 to 60 of about 1,798,469 (249)

An HflX-type GTPase from Sulfolobus solfataricus binds to the 50S ribosomal subunit in all nucleotide-bound states [PDF]

open access: yes, 2011
HflX GTPases are found in all three domains of life, Bacteria, Archaea, and Eukaryotes. HflX from Escherichia coli has been shown to bind to the 50S ribosomal subunit in a nucleotide-dependent manner and this interaction strongly stimulates its GTPase ...
Fabian Blombach   +27 more
core   +1 more source

Nutrient/TOR signaling controls adipose mitochondrial transcription factor A (TFAM) to regulate organismal growth in Drosophila

open access: yesFEBS Letters, EarlyView.
Animals must match their growth rate to available nutrients. We show that in Drosophila larvae, the nutrient‐sensing TOR kinase controls growth by regulating levels of TFAM, a key regulator of mitochondrial function, in the adipose tissue. When nutrients are abundant, high TOR activity suppresses TFAM, lowering mitochondrial bioenergetic activity and ...
Shrivani Sriskanthadevan‐Pirahas   +4 more
wiley   +1 more source

Structure and function of bacterial dynamin-like proteins [PDF]

open access: yes, 2012
Membrane dynamics are essential for numerous cellular processes in eukaryotic and prokaryotic cells. In eukaryotic cells, membrane fusion and fission are often catalyzed by large GTPases of the dynamin protein family. These proteins couple GTP hydrolysis
Bramkamp, Marc
core   +1 more source

Peripheral lysosomes recruit PLEKHG3 to focal adhesions and restrain protrusion dynamics

open access: yesFEBS Letters, EarlyView.
Proximity‐dependent labeling at the LAMTOR complex revealed the Rho GEF PLEKHG3 as a lysosome‐proximal protein directing the study toward the influence of lysosome positioning on actin dynamics and cell motility. We show that PLEKHG3 colocalizes with lysosomes at focal adhesion sites and observe that forced peripheral dispersion of lysosomes hinders ...
Rainer Ettelt   +8 more
wiley   +1 more source

Substrate binding disrupts dimerization and induces nucleotide exchange of the chloroplast GTPase Toc33

open access: yes, 2011
GTPases act as molecular switches to control many cellular processes, including signalling, protein translation and targeting. Switch activity can be regulated by external effector proteins or intrinsic properties, such as dimerization.
Ivo Tews   +19 more
core   +1 more source

VAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase [PDF]

open access: yes, 2014
Background: FAF1 is a ubiquitin-binding adaptor for the p97 ATPase and belongs to the UBA-UBX family of p97 cofactors. p97 converts the energy derived from ATP hydrolysis into conformational changes of the p97 hexamer, which allows the dissociation of ...
Tyagi, Kshitiz   +15 more
core   +1 more source

Golgi enzymes are retrieved from the plasma membrane to the trans‐Golgi network

open access: yesFEBS Letters, EarlyView.
Golgi enzymes are traditionally considered resident proteins retained within the Golgi apparatus. Here, we demonstrate that a subset transiently reaches the cell surface and is subsequently retrieved to the trans‐Golgi network via retrograde transport. Using a nanobody‐based toolkit, we uncover a dynamic trafficking cycle of several Golgi enzymes.
Dominik P. Buser, Tina Junne
wiley   +1 more source

The interaction of Ras with GTPase-activating proteins [PDF]

open access: yes, 1997
Ras plays a major role as a molecular switch in many signal transduction pathways which lead to cell growth and differentiation. The GTPase reaction of Ras is of central importance in the function of the switch since it terminates Ras-effector ...
Wittinghofer, A.   +8 more
core   +1 more source

The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation

open access: yesFEBS Letters, EarlyView.
Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge   +6 more
wiley   +1 more source

IDENTIFICATION AND PARTIAL-PURIFICATION OF GTPASE-ACTIVATING PROTEINS FROM YEAST AND MAMMALIAN-CELLS THAT PREFERENTIALLY ACT ON YPT1/RAB1 PROTEINS [PDF]

open access: yes, 1991
Two GTPase-activating proteins of apparent molecular mass of 100 kDa and 30 kDa have been partially purified from porcine liver cytosol usinig mammalian Ypt1/Rab1 protein as substrate.
Tan, Tjie J.   +9 more
core   +1 more source

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