Search results for "COPII"
showing 9 items of 19 documents
High‐Resolution X‐Ray Spectroscopy of the Post–T Tauri Star PZ Telescopii
2004
We present an analysis of the Chandra High Energy Transmission Grating Spectrometer observation of the rapidly rotating P_(rot)=0.94 d post T Tauri (~20 Myr old) star PZ Telescopii, in the Tucana association. Using two different methods we have derived the coronal emission measure distribution, em(T), and chemical abundances. The em(T) peaks at log T = 6.9 and exhibits a significant emission measure at temperatures log T > 7. The coronal abundances are generally ~0.5 times the solar photospheric values that are presumed fairly representative of the composition of the underlying star. A minimum in abundance is seen at a first ionization potential (FIP) of 7-8 eV, with evidence for higher abu…
Putative p24 complexes in Arabidopsis contain members of the delta and beta subfamilies and cycle in the early secretory pathway
2013
p24 proteins are a family of type I membrane proteins localized to compartments of the early secretory pathway and to coat protein I (COPI)- and COPII-coated vesicles. They can be classified, by sequence homology, into four subfamilies, named p24α, p24β, p24γ, and p24δ. In contrast to animals and fungi, plants contain only members of the p24β and p24δ subfamilies, the latter probably including two different subclasses. It has previously been shown that transiently expressed red fluorescent protein (RFP)-p24δ5 (p24δ1 subclass) localizes to the endoplasmic reticulum (ER) at steady state as a consequence of highly efficient COPI-based recycling from the Golgi apparatus. It is now shown that tr…
Coupled transport of Arabidopsis p24 proteins at the ER–Golgi interface
2012
p24 proteins are a family of type I membrane proteins localized to compartments of the early secretory pathway and to coat protein I (COPI)- and COPII-coated vesicles. They can be classified, by sequence homology, into four subfamilies, named p24α, p24β, p24γ, and p24δ. In contrast to animals and fungi, plants contain only members of the p24β and p24δ subfamilies. It has previously been shown that transiently expressed red fluorescent protein (RFP)–p24δ5 localizes to the endoplasmic reticulum (ER) as a consequence of highly efficient COPI-based recycling from the Golgi apparatus. Using specific antibodies, endogenous p24δ5 has now been localized to the ER and p24β2 to the Golgi apparatus in…
Tráfico intracelular de proteínas de la familia p24 en células vegetales
2014
Las proteínas p24 constituyen una familia única de proteínas transmembrana de tipo I, con un peso molecular aproximado de 24 kDa, que se localizan mayoritariamente en los compartimentos de la vía secretora temprana, retículo endoplásmico (ER) y complejo de Golgi, y son componentes mayoritarios de las vesículas recubiertas por proteínas COPI o COPII. Se dividen, por homología de secuencia, en cuatro subfamilias: p24α, p24β, p24δ y p24γ. En animales y levaduras hay representantes de cada una de las 4 subfamilias; sin embargo, las plantas solo tienen miembros de la subfamilia p24β y p24δ. En Arabidopsis existen 9 miembros de la subfamilia p24δ (p24δ3-p24δ11) y 2 de la subfamilia p24β (p24β2 y …
Arabidopsis p24δ5 and p24δ9 facilitate Coat Protein I-dependent transport of the K/HDEL receptor ERD2 from the Golgi to the endoplasmic reticulum.
2014
The p24 proteins belong to a family of type I membrane proteins which cycle between the endoplasmic reticulum (ER) and Golgi via coat protein I (COPI) and COPII vesicles. Current nomenclature classifies them into four subfamilies, although plant p24 proteins belong to either the p24β or the p24δ subfamilies. Here, we show that Arabidopsis p24δ5/δ9 and HDEL ligands shift the steady-state distribution of the K/HDEL receptor ERD2 from the Golgi to the ER. We also show that p24δ5/δ9 interact directly with ERD2. This interaction requires the Golgi dynamics (GOLD) domain in p24δ5 and is much higher at acidic than at neutral pH, consistent with both proteins interacting at the cis-Golgi. In additi…
In vivo Trafficking and Localization of p24 Proteins in Plant Cells
2008
p24 proteins constitute a family of putative cargo receptors that traffic in the early secretory pathway. p24 proteins can be divided into four subfamilies (p23, p24, p25 and p26) by sequence homology. In contrast to mammals and yeast, most plant p24 proteins contain in their cytosolic C-terminus both a dilysine motif in the -3, -4 position and a diaromatic motif in the -7, -8 position. We have previously shown that the cytosolic tail of Arabidopsis p24 proteins has the ability to interact with ARF1 and coatomer (through the dilysine motif) and with COPII subunits (through the diaromatic motif). Here, we establish the localization and trafficking properties of an Arabidopsis thaliana p24 pr…
Function of AtPGAP1 in GPI anchor lipid remodeling and transport to the cell surface of GPI-anchored proteins
2021
ABSTRACTGPI-anchored proteins (GPI-APs) play an important role in a variety of plant biological processes including growth, stress response, morphogenesis, signalling and cell wall biosynthesis. The GPI-anchor contains a lipid-linked glycan backbone that is synthesized in the endoplasmic reticulum (ER) where it is subsequently transferred to the C-terminus of proteins containing a GPI signal peptide by a GPI transamidase. Once the GPI anchor is attached to the protein, the glycan and lipid moieties are remodelled. In mammals and yeast, this remodelling is required for GPI-APs to be included in Coat Protein II (COPII) coated vesicles for their ER export and subsequent transport to the cell s…
Endoplasmic Reticulum stress reduces COPII vesicle formation and modifies Sec23a cycling at ERESs
2013
AbstractExit from the Endoplasmic Reticulum (ER) of newly synthesized proteins is mediated by COPII vesicles that bud from the ER at the ER Exit Sites (ERESs). Disruption of ER homeostasis causes accumulation of unfolded and misfolded proteins in the ER. This condition is referred to as ER stress. Previously, we demonstrated that ER stress rapidly impairs the formation of COPII vesicles. Here, we show that membrane association of COPII components, and in particular of Sec23a, is impaired by ER stress-inducing agents suggesting the existence of a dynamic interplay between protein folding and COPII assembly at the ER.
Modèle des voies réflexes et cérébelleuses, permettant le calcul de fonctions inverses et la commande d'un segment mécanique mobile
2004
14/07/2004; La commande et le contrôle des mouvements des membres par les voies cérébelleuses et réflexes sont modélisées au moyen d'un circuit dont la structure est déduite de contraintes fonctionnelles. 1/ La première contrainte est que les mouvements rapides des membres doivent être précis, quoiqu'ils ne puissent pas être commandés en boucle fermée au moyen de signaux sensoriels. Les voies qui préparent les ordres moteurs doivent donc contenir des fonctions inverses approximées des fonctions biomécaniques du membre et des muscles. Or une telle fonction peut être calculée au moyen de boucles de rétroaction parallèles, dont la structure est comparable à l'anatomie des voies cérébelleuses. …