Clathrin assembles into honeycomb-like lattices at the plasma membrane but also on internal membranes, such as at the Golgi and tubular endosomes. Clathrin assemblies primarily regulate the intracellular trafficking of different cargoes, but clathrin also has non-endocytic functions in cell adhesion through interactions with specific integrins, contributes to intraluminal vesicle formation by forming flat bilayered coats on endosomes and even assembles on kinetochore k-fibers during mitosis. In this Cell Science at a Glance article and the accompanying poster, we review our current knowledge on the different types of canonical and non-canonical membrane-associated clathrin assemblies in mammalian cells, as observed by thin-section or platinum replica electron microscopy in various cell types, and discuss how the structural plasticity of clathrin contributes to its functional diversity.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1242/jcs.261674 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
The nanoscale organization of the Nipah virus fusion protein informs new membrane fusion mechanisms.
Elife
January 2025
Institute of Parasitology, Faculty of Agricultural and Environmental Sciences, McGill University, Montreal, Canada.
Paramyxovirus membrane fusion requires an attachment protein for receptor binding and a fusion protein for membrane fusion triggering. Nipah virus (NiV) attachment protein (G) binds to ephrinB2 or -B3 receptors, and fusion protein (F) mediates membrane fusion. NiV-F is a class I fusion protein and is activated by endosomal cleavage.
View Article and Find Full Text PDFFast-diffusing receptor collisions with slow-diffusing peptide ligand assemble the ternary parathyroid hormone-GPCR-arrestin complex.
Nat Commun
December 2024
Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, 15261, USA.
Article Synopsis
- - The study investigates how a peptide hormone (PTH) interacts with its receptor (PTHR) and β-arrestin (βarr) to form a ternary complex, which is key for G protein-coupled receptor (GPCR) signaling.
- - Using fluorescent markers and advanced imaging techniques, the research shows that PTHR moves freely in the cell membrane while unbound PTH has limited mobility, indicating a distinct dynamic behavior.
- - The formation of the PTH-PTHR-βarr complex happens in three steps: ligand-receptor collisions, βarr recruitment triggered by a specific lipid (PIP), and final assembly within clathrin clusters, highlighting the importance of PIP in GPCR
Haploinsufficiency and Alzheimer's Disease: The Possible Pathogenic and Protective Genetic Factors.
Int J Mol Sci
November 2024
Department of Bionano Technology, Gachon Medical Research Institute, Gachon University, Seongnam 13120, Republic of Korea.
Alzheimer's disease (AD) is a complex neurodegenerative disorder influenced by various genetic factors. In addition to the well-established amyloid precursor protein (), Presenilin-1 (), Presenilin-2 (), and apolipoprotein E (), several other genes such as Sortilin-related receptor 1 (), Phospholipid-transporting ATPase ABCA7 (), Triggering Receptor Expressed on Myeloid Cells 2 (), Phosphatidylinositol-binding clathrin assembly protein (), and clusterin () were implicated. These genes contribute to neurodegeneration through both gain-of-function and loss-of-function mechanisms.
View Article and Find Full Text PDFIntersectin1 promotes clathrin-mediated endocytosis by organizing and stabilizing endocytic protein interaction networks.
Cell Rep
December 2024
Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA. Electronic address:
During clathrin-mediated endocytosis (CME), dozens of proteins are recruited to nascent CME sites on the plasma membrane, and their spatial and temporal coordination is crucial for efficient CME. Here, we show that the scaffold protein intersectin1 (ITSN1) promotes CME by organizing and stabilizing endocytic protein interaction networks. Live-cell imaging of genome-edited cells revealed that endogenously labeled ITSN1 is recruited during CME site stabilization and growth and that ITSN1 knockdown impairs endocytic protein recruitment during this stage.
View Article and Find Full Text PDFStructural basis of pseudoGTPase-mediated protein-protein interactions.
bioRxiv
November 2024
Department of Biological Science, Florida State University, Tallahassee, FL 32306, USA.
Article Synopsis
- GTPases control various cellular functions by changing shape when they bind to GTP or GDP, while pseudoGTPases, which are inactive versions, are less understood despite being found in many organisms.
- This study identifies the N-terminal region of AAGAB as a type I pseudoGTPase using biochemical methods and X-ray crystallography, revealing its role in cellular processes.
- The research shows that the pseudoGTPase domain of AAGAB uniquely interacts with σ subunits of AP1 and AP2 complexes, essential for transporting materials in cells, highlighting the importance of this interaction interface for membrane trafficking.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!