• Membrane bound Sar1 attracts the Sec23-Sec24 protein heterodimer to the ER membrane. (wikipedia.org)
  • Activation of the GTPase also reverses the interaction between Sar1 and the Sec23-Sec24 protein dimer. (wikipedia.org)
  • The protein encoded by this gene is a member of the SEC23 subfamily of the SEC23/SEC24 family, which is involved in vesicle trafficking. (nih.gov)
  • This gelsolin-like domain can also be found in the C-terminal of the members of Sec23/Sec24 family. (embl.de)
  • protein transporter SEC24;Sec23/Sec24 beta-sandwich. (ntu.edu.sg)
  • Two types of coatomers are known: COPI (retrograde transport from trans-Golgi network to cis-Golgi network and endoplasmic reticulum) COPII (anterograde transport from ER to the cis-Golgi) Coatomers are functionally analogous and evolutionarily homologous to clathrin adaptor proteins, also known as adaptins, which regulate endocytosis from the plasma membrane and transport from the trans-Golgi network to lysosomes. (wikipedia.org)
  • Secretory proteins exit the endoplasmic reticulum (ER) in coat protein complex II (COPII)-coated vesicles and then progress through the Golgi complex before delivery to their final destination. (biologists.com)
  • They are components of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). (embl.de)
  • I am a plant cell biologist and protein biochemist at Oxford Brookes University with expertise in the structure and function of the plant endoplasmic reticulum (ER), membrane proteins and auxin biosynthesis using biochemical techniques as well as high-resolution live cell imaging. (brookes.ac.uk)
  • The encoded protein has similarity to yeast Sec23p component of COPII. (nih.gov)
  • COPII is the coat protein complex responsible for vesicle budding from the ER. (nih.gov)
  • vesicle coat complex COPII, subunit Sec24 family. (ntu.edu.sg)
  • COPII-coated vesicle component Sfb3 (predicted). (ntu.edu.sg)
  • The coat on the budding vesicle comprises two layers, an inner layer of adaptor proteins (gray ovals) and an outer layer that forms a polyhedral cage. (biologists.com)
  • COPI is a coatomer that coats the vesicles transporting proteins from the Golgi complex to the ER. (wikipedia.org)
  • Before the COP I protein can coat vesicles on the Golgi membrane, it must interact with a small GTPase called ARF1 (ADP ribosylation factor). (wikipedia.org)
  • ARF1 that is bound to GDP interacts with the golgi complex membrane. (wikipedia.org)
  • Next, guanine nucleotide exchange factors (GEFs) in the golgi complex membrane exchange the GDP bound to ARF1 for GTP. (wikipedia.org)
  • This activates ARF1, allowing it to insert an amphipathic alpha helix into the lipid bilayer of the Golgi complex. (wikipedia.org)
  • Next, the ARF1 protein recruits COP1 to the golgi complex membrane by interacting with β-COP and γ-COP. (wikipedia.org)
  • COP II vesicles must shed their coat before they can fuse with the cis-Golgi membrane. (wikipedia.org)
  • Newly made secretory proteins must pass through the ER and the golgi complex before they can leave the cell. (wikipedia.org)
  • PolyGA expression up-regulated proteins involved in ER to Golgi trafficking, and down-regulated proteins involved in insulin signalling. (biomedcentral.com)
  • KKXX signals are associated with transmembrane ER domains and KDEL signals are associated with proteins in the ER lumen. (wikipedia.org)
  • Sar1 directly binds to Sec23 while Sec24 directly binds to the cargo receptor located on the ER membrane. (wikipedia.org)
  • In addition, this protein binds with high affinity to fibronectin. (embl.de)
  • The coatomer is a protein complex that coats membrane-bound transport vesicles. (wikipedia.org)
  • COP1 coated vesicles also contain p24 proteins that assist with cargo sorting. (wikipedia.org)
  • COP II vesicles select the proper cargo by directly interacting with ER export signals that are present in transmembrane ER proteins. (wikipedia.org)
  • The COP1 proteins recognize the proper cargo by interacting with sorting signals on the cytoplasmic domains of the protein. (wikipedia.org)
  • This process depends on the general physico-chemical features of the cargo membrane protein and on the interactions of these features with the collective properties of the bilayer, instead of the one-to-one intermolecular interactions that exist between discrete signals and their receptors. (biologists.com)
  • For membrane proteins, a third mechanism, based on the interaction of their transmembrane domain (TMD) with lipid microdomains, must also be considered. (biologists.com)
  • protein_coding" "Cz01g27080.t1","No alias","Chromochloris zofingiensis","Solute-binding protein family 5 domain [Interproscan]. (ntu.edu.sg)
  • protein_coding" "Cz02g09110.t1","No alias","Chromochloris zofingiensis","2-hydroxy-palmitic acid dioxygenase Mpo1-like [Interproscan]. (ntu.edu.sg)
  • protein_coding" "Cz03g01030.t1","No alias","Chromochloris zofingiensis","Rieske [2Fe-2S] iron-sulphur domain [Interproscan]. (ntu.edu.sg)
  • This gene plays an important role in regulating the transport of proteins within cells. (wikipedia.org)
  • Our study thus uncovers a previously unrecognized hierarchical regulatory mechanism in which an E3 ubiquitin ligase targets a peroxisome receptor protein that negatively regulates immunity in rice by stabilizing an aldehyde dehydrogenase that suppresses defense gene expression. (bvsalud.org)
  • The receptor protein PEX5, an important component of peroxisomes, regulates growth, development, and immunity in yeast and mammals. (bvsalud.org)
  • G protein-coupled receptor 37. (gsea-msigdb.org)
  • In this Commentary, I review evidence in favor of the idea that partitioning of TMDs into bilayer domains that are endowed with distinct physico-chemical properties plays a pivotal role in the transport of membrane proteins within the early secretory pathway. (biologists.com)
  • The combination of such self-organizational phenomena with canonical intermolecular interactions is most likely to control the release of membrane proteins from the ER into the secretory pathway. (biologists.com)
  • Program access grant to the STFC Harwell Laser Facility 'The Plant Cell Initiative: Protein interactions in the higher plant secretory pathway' 2017-2021 (approximate value of £200K). (brookes.ac.uk)
  • This complex polymerizes to form the outer layer of the coat. (wikipedia.org)
  • Once Sar1 interacts with the ER membrane, a membrane protein called Sec12 acts a guanine nucleotide exchange factor and substitutes GTP for GDP on Sar1. (wikipedia.org)
  • This activates the Sar1 protein, causing its amphipathic alpha helix to bind to the ER membrane. (wikipedia.org)
  • I took up a position at Oxford Brookes University in 2012 investigating the role of reticulon proteins in ER tubulation and viral trafficking in order to develop my international reputation in ER research and advanced imaging. (brookes.ac.uk)
  • I am committed to interdisciplinary research, and an example of the successes gained from this approach is the project with Prof A Nabok (Engineering Sheffield Hallam University) using total internal reflection ellipsometry to quantify protein-membrane interactions on native plant membranes and human cell lines. (brookes.ac.uk)
  • ARF-GAP1 is responsible for deactivating the ARF1 protein by activating the GTPase. (wikipedia.org)
  • SCOPE: Substituting plant protein for animal protein has emerged as a promising strategy for managing atherogenic lipids. (bvsalud.org)
  • However, the impact of long-term intake of a high plant protein diet (HPD) on hepatic lipid disorder remains unclear. (bvsalud.org)
  • CONCLUSION: Diet rich in plant protein diet alleviates hyperlipidemia via increased microbial production of 12,13-DiHOME. (bvsalud.org)
  • I published the first report of plant ER reticulon protein interactors by Co-IP and FRET-FLIM. (brookes.ac.uk)
  • In summary, our data show that long polyGA proteins can be highly toxic in vivo, and that they may therefore contribute to ALS/FTD pathogenesis in patients. (biomedcentral.com)