Zobrazeno 1 - 10
of 74
pro vyhledávání: '"KKXX"'
Publikováno v:
BMC Molecular and Cell Biology, Vol 22, Iss 1, Pp 1-11 (2021)
BMC Molecular and Cell Biology
BMC Molecular and Cell Biology
Background Cisd1 and Cisd2 proteins share very similar structures with an N-terminal membrane-anchoring domain and a C-terminal cytosolic domain containing an iron-cluster binding domain and ending with a C-terminal KKxx sequence. Despite sharing a s
Autor:
Peter I. Mackenzie, Keiko Fujimoto, Akane Kimura, Shinji Takechi, Yoshitaka Tanaka, Yuji Ishii, Ken Kurohara, Madoka Esaki, Yuko Hirota, Yuu Miyauchi
Publikováno v:
Drug Metabolism and Pharmacokinetics. 35:466-474
UDP-Glucuronosyltransferase (UGT) is a type I membrane protein localized to the endoplasmic reticulum (ER). UGT has a di-lysine motif (KKXX/KXKXX) in its cytoplasmic domain, which is defined as an ER retention signal. However, our previous study has
Autor:
Samo Roškar, Tina Fink, Arne Praznik, Nina Jerala, Jan Lonzarić, Nik Franko, Roman Jerala, Tjaša Plaper, Mojca Benčina
Publikováno v:
Nature communications. 13(1)
Secreted proteins, such as hormones or cytokines, are key mediators in multicellular organisms. Protein secretion based on transcriptional control is rather slow, as proteins requires transcription, translation, followed by the transport from the end
Autor:
Peter I. Mackenzie, Keiko Fujimoto, Akane Kimura, Yuu Miyauchi, Yoshitaka Tanaka, Yuji Ishii, Sora Kimura, Yuko Hirota, Ken Kurohara
Publikováno v:
Molecular Pharmacology. 95:551-562
UDP-Glucuronosyltransferase (UGT) plays an important role in the metabolism of endogenous and exogenous compounds. UGT is a type I membrane protein, and has a dilysine motif (KKXX/KXKXX) in its C-terminal cytoplasmic domain. Although a dilysine motif
Publikováno v:
Journal of Virology
Porcine epidemic diarrhea virus (PEDV) causes high mortality in neonatal piglets. The PEDV spike (S) protein contains two intracellular sorting motifs, YxxΦ (tyrosine-based motif YEVF or YEAF) and KVHVQ at the cytoplasmic tail, yet their functions h
Publikováno v:
Mycobiology
Eukaryotic cells contain a collection of spatially separated internal organelles embedded in the cytoplasm. Communication between these internal organelles is mediated by trafficking events that are mainly accomplished by vesicular transport. These t
Autor:
Liwen Jiang, Byung-Ho Kang, Fernando Aniento, Yi Cai, Caiji Gao, Yejun Wang, David G. Robinson
Publikováno v:
Trends in Plant Science. 19:508-515
Unless there are mechanisms to selectively retain membrane proteins in the endoplasmic reticulum (ER) or in the Golgi apparatus, they automatically proceed downstream to the plasma or vacuole membranes. Two types of coat protein complex I (COPI)-inte
Enhanced secretion of a methyl parathion hydrolase in Pichia pastoris using a combinational strategy
Publikováno v:
Microbial Cell Factories
Although Pichia pastoris has been successfully used to produce various recombinant heterologous proteins, the efficiency varies. In this study, we used methyl parathion hydrolase (MPH) from Ochrobactrum sp. M231 as an example to study the effect of p
Autor:
Jonathan Goldberg, Wenfu Ma
Publikováno v:
The EMBO Journal
Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α-COP and β'-COP subunits and packaged into COPI-coated vesicles for Golgi-to-ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their re
Autor:
Philip R. Evans, Lauren P. Jackson, Michael J. Lewis, Rainer Duden, Helen M. Kent, Melissa A. Edeling, David J. Owen
Publikováno v:
Developmental Cell
Summary COPI mediates retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) and within the Golgi stack, sorting transmembrane proteins bearing C-terminal KKxx or KxKxx motifs. The structure of KxKxx motifs bound to the N-terminal WD