Clathrin-independent endocytosis: Difference between revisions
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While clathrin-coated endocytosis is the most efficient and dominant means of cellular entry, endocytic pathways can operate without the presence of the clathrin triskelion. In the absence of clathrin, there are many elements of response that allow for the internalization of essential molecules to cellular function. |
While clathrin-coated endocytosis is the most efficient and dominant means of cellular entry, endocytic pathways can operate without the presence of the clathrin triskelion. In the absence of clathrin, there are many elements of response that allow for the internalization of essential molecules to cellular function. |
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== Mechanisms of Clathrin- |
== Mechanisms of Clathrin-Independent Carriers == |
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The mechanisms of clathrin-independent endocytosis can be separated into dynamin dependent and dynamin independent. Others have their own separate pathways completely. |
The mechanisms of clathrin-independent endocytosis can be separated into [[dynamin]] dependent and dynamin independent. Others have their own separate pathways completely. |
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=== Dynamin |
=== Dynamin Dependent === |
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==== Caveolar ==== |
==== Caveolar ==== |
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Caveolar dynamin-dependent endocytosis relies of [[caveolae]], which are invaginations of the cell plasma membrane made up of GPI-anchored proteins, sphingolipids, and cholesterol<ref>{{Cite journal |last=Mayor |first=Satyajit |last2=Pagano |first2=Richard E. |date=2007-08 |title=Pathways of clathrin-independent endocytosis |url=https://www.nature.com/articles/nrm2216 |journal=Nature Reviews Molecular Cell Biology |language=en |volume=8 |issue=8 |pages=603–612 |doi=10.1038/nrm2216 |issn=1471-0080}}</ref>. |
Caveolar dynamin-dependent endocytosis relies of [[caveolae]], which are invaginations of the cell plasma membrane made up of GPI-anchored proteins, sphingolipids, and cholesterol<ref name=":1">{{Cite journal |last=Mayor |first=Satyajit |last2=Pagano |first2=Richard E. |date=2007-08 |title=Pathways of clathrin-independent endocytosis |url=https://www.nature.com/articles/nrm2216 |journal=Nature Reviews Molecular Cell Biology |language=en |volume=8 |issue=8 |pages=603–612 |doi=10.1038/nrm2216 |issn=1471-0080}}</ref>. |
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==== RhoA-regulated ==== |
==== RhoA-regulated ==== |
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RhoA is a small [[GTPase]] mechanism that aids in the correct sorting of the beta chain of the interleukin-2-receptor ([[IL2RB|IL-2R-B]]). This pathway is know to be a key player in the dynamics of actin cytoskeleton dynamics and for recruiting actin machinery in other endocytic pathways as well<ref name=":1" />. |
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=== Dynamin |
=== Dynamin Independent === |
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==== CDC42-regulated ==== |
==== CDC42-regulated ==== |
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CDC42-regulated dynamin independent pathways are the main route of non-clathrin, non-caveolar uptake of fluid-phase internalization. Most CDC42-regulated endocytic pathways have large and wide surface invaginations and sometimes involves the recruitment of actin-polymerization machinery that further aid in the pinching off of the vesicle wall<ref name=":1" />. |
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==== ARF6-regulated ==== |
==== ARF6-regulated ==== |
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====== Role of Glycolipid-Lectin ====== |
====== Role of Glycolipid-Lectin ====== |
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Glycolipid-lectin, of the galectin family, facilitate tubular endocytic pits drive CLIC/GEEC endocytosis. Glycolipid-lectin binds onto cargo via a carbohydrate, and oligomerizes. This oligomerization allows the Glycolipid-lectin-protein-cargo complex to interact with glycosphingolipid(GSL)-binding subunits and causes a bending of the membrane<ref name=":0" />. Proteins like [[galectin-3]], [[Galectin-8|galectin 8]], and GSL-dependent cellular endocytosis of CD166 are all known to use Glycolipid-lectin. |
Glycolipid-lectin, of the [[galectin]] family, facilitate tubular endocytic pits drive CLIC/GEEC endocytosis. Glycolipid-lectin binds onto cargo via a carbohydrate, and oligomerizes. This oligomerization allows the Glycolipid-lectin-protein-cargo complex to interact with glycosphingolipid(GSL)-binding subunits and causes a bending of the membrane<ref name=":0" />. Proteins like [[galectin-3]], [[Galectin-8|galectin 8]], and GSL-dependent cellular endocytosis of CD166 are all known to use Glycolipid-lectin. |
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==References== |
==References== |
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Revision as of 19:43, 11 April 2024
Overview
Clathrin-independent carriers (CLICs) are prevalent tubulovesicular membranes responsible for non-clathrin mediated endocytic events. They appear to endocytose material into GPI-anchored protein-enriched early endosomal compartment (GEECs). Collectively, CLICs and GEECs comprise the Cdc42-mediated CLIC/GEEC endocytic pathway, which is regulated by GRAF1.[1][2][3]
While clathrin-coated endocytosis is the most efficient and dominant means of cellular entry, endocytic pathways can operate without the presence of the clathrin triskelion. In the absence of clathrin, there are many elements of response that allow for the internalization of essential molecules to cellular function.
Mechanisms of Clathrin-Independent Carriers
The mechanisms of clathrin-independent endocytosis can be separated into dynamin dependent and dynamin independent. Others have their own separate pathways completely.
Dynamin Dependent
Caveolar
Caveolar dynamin-dependent endocytosis relies of caveolae, which are invaginations of the cell plasma membrane made up of GPI-anchored proteins, sphingolipids, and cholesterol[4].
RhoA-regulated
RhoA is a small GTPase mechanism that aids in the correct sorting of the beta chain of the interleukin-2-receptor (IL-2R-B). This pathway is know to be a key player in the dynamics of actin cytoskeleton dynamics and for recruiting actin machinery in other endocytic pathways as well[4].
Dynamin Independent
CDC42-regulated
CDC42-regulated dynamin independent pathways are the main route of non-clathrin, non-caveolar uptake of fluid-phase internalization. Most CDC42-regulated endocytic pathways have large and wide surface invaginations and sometimes involves the recruitment of actin-polymerization machinery that further aid in the pinching off of the vesicle wall[4].
ARF6-regulated
Fast Endophilin-Mediated Endocytosis
Fast endophilin-mediated endocytosis is a form of clathrin-independent endocytosis uses cargo capture by cytolytic proteins to allow for endophilin and receptor endocytosis.[5]
Endophilin is typically bound in distinct patches to the plasma membrane by lamellipodin. However, without receptor activation, these patches disassemble, typically within 5-10 seconds, and move to a new, random, nearby location to reassemble, The complex continues to probe the membrane until the correct ligand binds and the cargo is sorted to a FEME carrier. While the exact mechanisms by which the receptors sorts the cargo to the specific carriers, it is suggested that during cargo capture, the endphillion levels rise to be greater than the critical concentration (Cc) and initiate bending of the membrane. It may also be possible that the binding of a ligand causes receptor clustering near the binding and causes a collapse or bending of the local membrane.[6]
CLIC/GEEC Endocytic Pathway
The clathrin-independent carrier pathway is the main pathway to endocytose cargo and relies heavily GPI-anchored proteins, integrins, and proteins to create membrane tension and fluidity. Crescent shaped tubular clathrin-independent carriers (CLICs) mature into glycosylphosphatidylinositol (GPI)-anchored protein-enriched early endocytic compartments(GEECs)[7].
Role of Glycolipid-Lectin
Glycolipid-lectin, of the galectin family, facilitate tubular endocytic pits drive CLIC/GEEC endocytosis. Glycolipid-lectin binds onto cargo via a carbohydrate, and oligomerizes. This oligomerization allows the Glycolipid-lectin-protein-cargo complex to interact with glycosphingolipid(GSL)-binding subunits and causes a bending of the membrane[5]. Proteins like galectin-3, galectin 8, and GSL-dependent cellular endocytosis of CD166 are all known to use Glycolipid-lectin.
References
- ^ Lundmark, R.; Doherty, G.J.; Howes, M.T.; et al. (November 2008). "The GTPase-Activating Protein GRAF1 Regulates the CLIC/GEEC Endocytic Pathway". Current Biology. 18 (22): 1802–8. doi:10.1016/j.cub.2008.10.044. PMC 2726289. PMID 19036340.
- ^ Rossatti, P.; Ziegler, L.; Schregle, R; et al. (November 2019). "Cdc42 Couples T Cell Receptor Endocytosis to GRAF1-Mediated Tubular Invaginations of the Plasma Membrane". Cells. 8 (11): 1388. doi:10.3390/cells8111388. PMC 6912536. PMID 31690048.
- ^ Elkin, S.R.; Lakoduk, A.M.; Schmid, S.L. (May 2016). "Endocytic pathways and endosomal trafficking: a primer". Wiener Medizinische Wochenschrift. 166 (7–8): 196–204. doi:10.1007/s10354-016-0432-7. PMC 4873410. PMID 26861668.
- ^ a b c Mayor, Satyajit; Pagano, Richard E. (2007-08). "Pathways of clathrin-independent endocytosis". Nature Reviews Molecular Cell Biology. 8 (8): 603–612. doi:10.1038/nrm2216. ISSN 1471-0080.
{{cite journal}}: Check date values in:|date=(help) - ^ a b Ferreira, Antonio P.A.; Boucrot, Emmanuel (2018-03). "Mechanisms of Carrier Formation during Clathrin-Independent Endocytosis". Trends in Cell Biology. 28 (3): 188–200. doi:10.1016/j.tcb.2017.11.004. ISSN 0962-8924.
{{cite journal}}: Check date values in:|date=(help) - ^ Ferreira, Antonio; Boucrot, Emmanuel (March 2018). "Mechanisms of Carrier Formation during Clathrin-Independent Endocytosis" (PDF). Cell Press Reviews. 28 (3).
{{cite journal}}: line feed character in|title=at position 39 (help) - ^ Shafaq-Zadah, Massiullah; Dransart, Estelle; Johannes, Ludger (2020-8). "Clathrin-independent endocytosis, retrograde trafficking, and cell polarity". Current Opinion in Cell Biology. 65: 112–121. doi:10.1016/j.ceb.2020.05.009. ISSN 0955-0674. PMC 7588825. PMID 32688213.
{{cite journal}}: Check date values in:|date=(help)