Article
Biochemistry & Molecular Biology
Boris Simonetti, Qian Guo, Manuel Gimenez-Andres, Kai-En Chen, Edmund R. R. Moody, Ashley J. Evans, Mintu Chandra, Chris M. Danson, Tom A. Williams, Brett M. Collins, Peter J. Cullen
Summary: This study elucidates how SNX27-Retromer promotes endosome-to-plasma membrane recycling through its interaction with the SNX-BAR sorting complex, and reveals the stepwise evolution of this complex during early metazoan evolution.
Article
Multidisciplinary Sciences
Jachen Solinger, Harun-Or Rashid, Anne Spang
Summary: Cellular organization, compartmentalization, and cell-to-cell communication rely on endosomal pathways, and FERARI plays a crucial role in coordinating these pathways and regulating cargo flow through sorting endosomes via a kiss-and-run mechanism.
NATURE COMMUNICATIONS
(2022)
Review
Cell Biology
Saara Laulumaa, Markku Varjosalo
Summary: The Commander complex is made up of 16 proteins and plays multiple roles in various intracellular events, cell homeostasis, cell cycle regulation, and immune response. These ubiquitously expressed proteins have been linked to diseases like Wilson's disease, atherosclerosis, and cancer. The Commander complex may play a more significant role in intracellular regulation than currently understood, requiring more systematic research.
Article
Biochemistry & Molecular Biology
Esra Cicek, Ayca Circir, Merve Oyken, Ozge Akbulut Caliskan, Didem Naz Dioken, Sezen Guntekin Ergun, Rengul Cetin-Atalay, Aysegul Sapmaz, Huib Ovaa, Ozgur Sahin, Ayse Elif Erson-Bensan
Summary: SNX3 plays a critical role in the EGFR network in triple-negative breast cancer, with increased interaction between SNX3 and EGFR upon EGF stimulation, affecting cell proliferation and migration, and correlating with relapse-free survival in breast cancer patients.
Article
Biochemistry & Molecular Biology
Thibault Courtellemont, Maria Giovanna De Leo, Navin Gopaldass, Andreas Mayer
Summary: Endo-lysosomal compartments exchange proteins through different processes, including fusion, fission, and endosomal transport carriers. The membrane fission events that occur during these processes are not well understood. This study identifies the CROP complex as a factor that plays a role in membrane fission. The CROP complex consists of members from two protein families and enhances the membrane fission activity of a specific protein. Disrupting the CROP complex prevents fragmentation of lysosome-like structures in yeast and impairs cargo export in mammalian endosomes.
Review
Multidisciplinary Sciences
Xin Yong, Lejiao Mao, Matthew N. J. Seaman, Da Jia
Summary: This review discusses the mechanisms of sorting and recognition of membrane proteins in endosomes, focusing on the role of the retromer complex and sorting nexin proteins. New data is highlighted on the importance of different sorting nexin proteins and how post-translational modifications can affect cargo sorting.
Article
Multidisciplinary Sciences
Kai-En Chen, Qian Guo, Timothy A. Hill, Yi Cui, Amy K. Kendall, Zhe Yang, Ryan J. Hall, Michael D. Healy, Joanna Sacharz, Suzanne J. Norwood, Sachini Fonseka, Boyang Xie, Robert C. Reid, Natalya Leneva, Robert G. Parton, Rajesh Ghai, David A. Stroud, David P. Fairlie, Hiroaki Suga, Lauren P. Jackson, Rohan D. Teasdale, Toby Passioura, Brett M. Collins
Summary: The retromer complex plays a crucial role in endosomal membrane trafficking and signaling. Novel macrocyclic peptides have been developed to modulate its function by specifically binding to different subunits and disrupting interactions with other factors. These peptides provide insights into retromer function and offer a new therapeutic avenue for targeting this complex.
Article
Multidisciplinary Sciences
Hongbo Li, Ruihua Huang, Yanglan Liao, Shuhong Yang, Bojin Feng, Hongting Qin, Jun Zhou, Yonglun Zeng, Jinbo Shen, Xiaohong Zhuang, Liwen Jiang, Marisa S. Otegui, Shengchun Zhang, Caiji Gao
Summary: The study identifies a plant-specific endosomal regulator, BLISTER (BLI), that interacts with the retromer complex and plays a crucial role in regulating endosomal trafficking in plants.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2022)
Article
Biochemistry & Molecular Biology
Navin Gopaldass, Maria Giovanna De Leo, Thibault Courtellemont, Vincent Mercier, Christin Bissig, Aurelien Roux, Andreas Mayer
Summary: Proteins exit from endosomes through retromer-coated tubular carriers, which affects cellular signaling, lysosomal biogenesis, and various diseases. The coat formation requires overcoming membrane tension. In this study, we investigated the dynamics and driving force of this process using yeast retromer, BAR-domain sorting nexins Vps5 and Vps17, and synthetic lipid tubules. The results showed that the coat forms a static tubular structure by bidirectional oligomerization, and high concentrations of sorting nexins constrict the membrane tubes. However, retromer oligomers are needed to drive constriction at lower concentrations.
Article
Cell Biology
Nan Liu, Kai Liu, Chonglin Yang
Summary: WDR91 is identified as an important factor in retromer-dependent recycling, promoting the interaction of Rab7 with SNX-retromer components and facilitating the formation of the endosomal retrieval subdomain.
JOURNAL OF CELL BIOLOGY
(2022)
Article
Cell Biology
Zhe Yang, Zhengyang Feng, Zebin Li, Rohan D. Teasdale
Summary: The mammalian retromer complex plays a role in multiple early endosome-associated trafficking pathways, depending on the sorting nexin (SNX) it is complexed with. Depletion of retromer subunit Vps35 was found to decrease EGFR protein levels and increase association with lysosomal compartments. This study suggests that the absence of retromer can interfere with early endosome-associated protein trafficking pathways and organelle maturation, leading to a prolonged association of EGFR within early endosomes.
Article
Biochemistry & Molecular Biology
Julian M. Carosi, Donna Denton, Sharad Kumar, Timothy J. Sargeant
Summary: The retromer complex regulates the fate of receptors in the endolysosomal system and plays a central role in metabolic processes. This review focuses on the assembly of retromer components and how it interacts with endosomal membranes to sort cargo receptors. The article also explores the regulation of retromer in different metabolic states and its involvement in various diseases and microbial infections.
MOLECULAR AND CELLULAR BIOLOGY
(2023)
Article
Cell Biology
Lisa Marquardt, Matthew Taylor, Florian Kramer, Kerstin Schmitt, Gerhard H. Braus, Oliver Valerius, Michael Thumm
Summary: The yeast PROPPIN Atg18 is a beta-propeller protein that binds to both phosphatidylinositol-3-phosphate (PtdIns3P) and PtdIns(3,5)P-2. It can induce membrane tubulation and fission through membrane insertion. Atg18 interacts with Vps35, a component of the retromer complex, and competes with sorting nexin proteins Vps5 and Vps17. Atg18-retromer is involved in vacuolar fragmentation during hyperosmotic stress.
Article
Cell Biology
Sarah D. Neuman, Erica L. Terry, Jane E. Selegue, Amy T. Cavanagh, Arash Bashirullah
Summary: The research identifies the crucial role of the retromer complex in recycling secretory granule membrane proteins in Drosophila larval salivary glands, shedding light on secretory granule maturation and neurodegenerative diseases. This study provides new insights into the function of the retromer complex in secretory cells and suggests that missorting of secretory cargo might contribute to the progression of neurodegenerative diseases.
DISEASE MODELS & MECHANISMS
(2021)
Article
Cell Biology
Kamilla M. E. Laidlaw, Katherine M. Paine, Daniel D. Bisinski, Grant Calder, Karen Hogg, Sophia Ahmed, Sally James, Peter J. O'Toole, Chris MacDonald
Summary: Cell surface protein trafficking is regulated in response to nutrient availability. Recycling of internalized protein and lipid cargoes is attenuated during glucose starvation, potentially due to changes in endosomal PI3K activity and the involvement of Gpa2.
MOLECULAR BIOLOGY OF THE CELL
(2022)
Article
Cell Biology
Mohamed Kodiha, Nabila Azad, Siwei Chu, Noah Crampton, Ursula Stochaj
Summary: This study reveals that oxidative stress induces the nuclear accumulation of RanBP1 and the signaling pathways mediated by EGFR and PKA play a role in regulating RanBP1 localization during stress. RanBP1 acts as a downstream effector of these signaling routes, positioning it at the intersection of important cellular signaling circuits.
EUROPEAN JOURNAL OF CELL BIOLOGY
(2024)
