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A Modular Design for the Clathrin- and Actin-Mediated Endocytosis Machinery
Open accessAbstract
Endocytosis depends on an extensive network of interacting proteins that execute a series of distinct subprocesses. Previously, we used live-cell imaging of six budding-yeast proteins to define a pathway for association of receptors, adaptors, and actin during endocytic internalization. Here, we analyzed the effects of 61 deletion mutants on the dynamics of this pathway, revealing functions for 15 proteins, and we analyzed the dynamics of 8 of these proteins. Our studies provide evidence for four protein modules that cooperate to drive coat formation, membrane invagination, actin-meshwork assembly, and vesicle scission during clathrin/actin-mediated endocytosis. We found that clathrin facilitates the initiation of endocytic-site assembly but is not needed for membrane invagination or vesicle formation. Finally, we present evidence that the actin-meshwork assembly that drives membrane invagination is nucleated proximally to the plasma membrane, opposite to the orientation observed for previously studied actin-assembly-driven motility processes.
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“Endocytosis typically requires force generation by active actin polymerization at the maturing endocytic pit52–57.”
From Membrane compression by synaptic vesicle exocytosis triggers ultrafast endocytosis (2023) · cites this paper as [54]
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“The Rvs proteins arrive after the actin marker Abp1p has started to accumulate but reach their peak fluorescence intensity together with Abp1p (Figures 6B and 6C), consistent with the timing of scission during mammalian endocytosis (Merrifield et al., 2005).”
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“In addition, cortical actin has been shown to control various steps of endocytosis by regulating, for example, membrane tension at the PM (Boulant et al., 2011) or vesicle scission (Kaksonen et al., 2005; Romer et al., 2010).”
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“Ede1p was hypothesized to be involved in endocytic site establishment because it affects the formation of productive endocytic sites (Kaksonen et al., 2005; Stimpson et al., 2009).”
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Sedwick, C. (2009) · Journal of Cell Biology · doi:10.1083/jcb.1846pi
ESTIMATING THE DURATION OF ENDOCYTIC EVENTS
Sebastián, R., Ayala, G., Díaz, M., Zoncu, R., & Toomre, D. (2007) · IEEE International Symposium on Biomedical Imaging · doi:10.1109/isbi.2007.356835
“Clathrin-mediated endocytosis is one of the best characterized endocytic routes [1, 2, 3].”
BackgroundActin-Based Feedback Circuits in Cell Migration and Endocytosis
Wang, X. (2016) · doi:10.7936/k7r20znv
“[72] showed that mutation of clathrin, which acts upstream of Las17, reduces the Las17 lifetime.”
BackgroundUsing fluorescence to study actomyosin in yeasts.
Mulvihill, D. P. (2014) · Experientia. Supplementum · doi:10.1007/978-3-0348-0856-9_13
Chae, M. (2013) · Rutgers University Community Repository (Rutgers University) · doi:10.7282/t3vm4b0q
Coupling Membrane Dynamics to Actin Polymerization
Suetsugu, S., & Takenawa, T. (2010) · Springer eBooks · doi:10.1007/978-90-481-9301-1_2
“The formation of clathrin-coated vesicles involves three steps ( Kaksonen et al., 2005; Merrifield et al., 2005).”
InfluentialActin in Clathrin-Mediated Endocytosis
Kaksonen, M. (2010) · Springer eBooks · doi:10.1007/978-90-481-9301-1_4
“Las17 and Pan1 localize independently of actin filaments, but the fourth NPF Abp1 localizes by binding to actin filaments at the endocytic site ( Kaksonen et al., 2005; Sun et al., 2006).”
BackgroundInfluentialSelf-citationThe role of toca-1-N-wasp complex in filopodia formation and endocytosis
Bu, W. (2010) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/41562
“This point is supported by the observation that transient actin polymerization is precisely coordinated with the recruitment of other endocytic proteins (Merrifield et al., 2002; Jonsdottir and Li, 2004; Kaksonen et al., 2003; Kaksonen et al., 2005; Merrifield et al., 2004; Merrifield et al., 2005; Newpher et al., 200…”
BackgroundBidirectional Crosstalk between Actin Dynamics and Endocytosis
Scita, G., & Fiore, P. P. D. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00305-3
Metadata
- Authors
- Kaksonen, M., Toret, C. P., & Drubin, D. G.
- Affiliations
- University of California, Berkeley (US)
- Corresponding author
- Drubin, David G.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2005-10
- Volume
- 123
- Issue
- 2
- Pages
- 305-320
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2106252068
- Cited by
- 726
- References
- 0
- Citations by year
- 2026: 10 · 2025: 18 · 2024: 15 · 2023: 22 · 2022: 35 · 2021: 23 · 2020: 27 · 2019: 24 · 2018: 37 · 2017: 26 · 2016: 31 · 2015: 34 · 2014: 40 · 2013: 50 · 2012: 45
- FWCI
- 17.18
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2882 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Sigrid Juséliuksen Säätiö
- National Institutes of Health (1s10rr019290-01)
- National Institute of General Medical Sciences (R01GM042759, R01GM050399)
- National Center for Research Resources (S10-RR019290)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- clathrin-mediated endocytosis, Saccharomyces cerevisiae, deletion mutants, protein modules, membrane invagination, vesicle scission, protein dynamics
- MeSH terms
- Red Fluorescent Protein, Actins, Carrier Proteins, Cell Membrane, Clathrin, Cytoskeletal Proteins, Endocytosis, Fungal Proteins, Kinetics, Luminescent Proteins, Membrane Glycoproteins, Microfilament Proteins, Models, Biological, Saccharomyces cerevisiae, Biomarkers, Gene Deletion, Clathrin-Coated Vesicles, Saccharomyces cerevisiae Proteins, Green Fluorescent Proteins, Actin Capping Proteins
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