A Pathway for Association of Receptors, Adaptors, and Actin during Endocytic Internalization
Open accessAbstract
In budding yeast, many proteins involved in endocytic internalization, including adaptors and actin cytoskeletal proteins, are localized to cortical patches of differing protein composition. Using multicolor real-time fluorescence microscopy and particle tracking algorithms, we define an early endocytic pathway wherein an invariant sequence of changes in cortical patch protein composition correlates with changes in patch motility. Three Arp2/3 activators each showed a distinct behavior, suggesting distinct patch-related endocytic functions. Actin polymerization occurs late in the endocytic pathway and is required both for endocytic internalization and for patch disassembly. In cells lacking the highly conserved endocytic protein Sla2p, patch motility was arrested and actin comet tails associated with endocytic patch complexes. Fluorescence recovery after photobleaching of the actin comet tails revealed that endocytic complexes are nucleation sites for rapid actin polymerization. Attention is now focused on the mechanisms by which the order and timing of events in this endocytic pathway are achieved.
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Endocytosis typically requires force generation by active actin polymerization at the maturing endocytic pit.
“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 [53]
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References 44 · Cited by 668
- Authors
- Kaksonen, M., Sun, Y., & Drubin, D. G.
- Affiliations
- University of California, Berkeley (US)
- Corresponding author
- Drubin, David G.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2003-11
- Volume
- 115
- Issue
- 4
- Pages
- 475-487
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2055188333
- Cited by
- 668
- References
- 44
- Citations by year
- 2026: 7 · 2025: 14 · 2024: 16 · 2023: 19 · 2022: 16 · 2021: 15 · 2020: 23 · 2019: 23 · 2018: 31 · 2017: 21 · 2016: 18 · 2015: 36 · 2014: 23 · 2013: 37 · 2012: 36
- FWCI
- 17.25
- 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, 3546 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
- National Institute of General Medical Sciences (GM42759, R01GM050399, GM-50399)
- 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 › Cellular Mechanics and Interactions
- Keywords
- actin polymerization, adaptor proteins, actin comet tails, Saccharomyces cerevisiae, endocytic pathway, actin cytoskeleton, particle tracking
- MeSH terms
- Actins, Algorithms, Carrier Proteins, Cytoskeletal Proteins, Endocytosis, Microscopy, Fluorescence, Receptors, Cell Surface, Saccharomyces cerevisiae, Transcription Factors, Receptors, Peptide, Two-Hybrid System Techniques, Transport Vesicles, Saccharomyces cerevisiae Proteins, Receptors, Mating Factor
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