scholarly journals Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis

2006 ◽  
Vol 172 (2) ◽  
pp. 269-279 ◽  
Author(s):  
Kazuya Tsujita ◽  
Shiro Suetsugu ◽  
Nobunari Sasaki ◽  
Masahiro Furutani ◽  
Tsukasa Oikawa ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Actin Cytoskeleton ◽  
Early Stage ◽  
Family Members ◽  
Protein Family ◽  
Membrane Deformation ◽  
Bar Domain ◽  
Cellular Processes ◽  
Cytoskeleton Reorganization ◽  
Membrane Tubulation

The conserved FER-CIP4 homology (FCH) domain is found in the pombe Cdc15 homology (PCH) protein family members, including formin-binding protein 17 (FBP17). However, the amino acid sequence homology extends beyond the FCH domain. We have termed this region the extended FC (EFC) domain. We found that FBP17 coordinated membrane deformation with actin cytoskeleton reorganization during endocytosis. The EFC domains of FBP17, CIP4, and other PCH protein family members show weak homology to the Bin-amphiphysin-Rvs (BAR) domain. The EFC domains bound strongly to phosphatidylserine and phosphatidylinositol 4,5-bisphosphate and deformed the plasma membrane and liposomes into narrow tubules. Most PCH proteins possess an SH3 domain that is known to bind to dynamin and that recruited and activated neural Wiskott-Aldrich syndrome protein (N-WASP) at the plasma membrane. FBP17 and/or CIP4 contributed to the formation of the protein complex, including N-WASP and dynamin-2, in the early stage of endocytosis. Furthermore, knockdown of endogenous FBP17 and CIP4 impaired endocytosis. Our data indicate that PCH protein family members couple membrane deformation to actin cytoskeleton reorganization in various cellular processes.

scholarly journals Regulation of caveolae through cholesterol-depletion dependent tubulation by PACSIN2/Syndapin II

2020 ◽  
Author(s):  
Aini Gusmira Amir ◽  
Kazuhiro Takemura ◽  
Kyoko Hanawa-Suetsugu ◽  
Kayoko Oono-Yakura ◽  
Kazuma Yasuhara ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Lipid Composition ◽  
Electrostatic Charge ◽  
Cholesterol Depletion ◽  
Membrane Deformation ◽  
Bar Domain ◽  
Caveolin 1 ◽  
Membrane Tubulation ◽  
Shaping Ability

AbstractThe membrane shaping ability of PACSIN2 via its FCH-BAR (F-BAR) domain has been shown to be essential for caveolar morphogenesis, presumably through the shaping of the caveolar neck. Caveolar membrane contains abundant levels of cholesterol. However, the role of cholesterol in PACSIN2-mediated membrane deformation remains unclear. We show that the binding of PACSIN2 to the membrane could be negatively regulated by the amount of cholesterol in the membrane. We prepared a reconstituted membrane based on the lipid composition of caveolae. The reconstituted membrane with cholesterol had a weaker affinity to the F-BAR domain of PACSIN2 than the membrane without cholesterol, presumably due to a decrease in electrostatic charge density. Consistently, the acute depletion of cholesterol from the plasma membrane resulted in the appearance of PACSIN2-localized tubules with caveolin-1 at their tips, suggesting that the presence of cholesterol inhibited the prominent membrane tubulation by PACSIN2. The tubules induced by PACSIN2 were suggested to be an intermediate of caveolae endocytosis. Consistently, the removal of caveolae from the plasma membrane upon cholesterol depletion was diminished in the cells deficient in PACSIN2. These data suggested that PACSIN2 mediated the caveolae internalization dependently on the amount of cholesterol at the plasma membrane, providing a possible mechanism for the cholesterol-dependent regulation of caveolae.

scholarly journals Novel roles for mammalian septins: from vesicle trafficking to oncogenesis

2001 ◽  
Vol 114 (5) ◽  
pp. 839-844 ◽  
Author(s):  
B. Kartmann ◽  
D. Roth
Keyword(s):  
Plasma Membrane ◽  
Recent Work ◽  
Cell Biology ◽  
Vesicle Trafficking ◽  
Family Members ◽  
Protein Family ◽  
Cellular Functions ◽  
Cellular Processes ◽  
Sequence Homologies ◽  
Genome Analyses

In recent years a convergence of various aspects of cell biology has become apparent, and yet investigators are only beginning to grasp the underlying unifying mechanisms. Among the proteins that participate in diverse aspects of cell biology are the septins. These are a group of novel GTPase proteins that are broadly distributed in many eukaryotes except plants. Although septins were originally identified as a protein family involved in cytokinesis in yeast, recent advances in the field have now ascribed additional functions to these proteins. In particular, the number of known mammalian septin family members has increased dramatically as more data has become available through genome analyses. We suggest a classification for the mammalian septins based on the sequence homologies in their highly divergent N- and C-termini. Recent work suggests novel functions for septins in vesicle trafficking, oncogenesis and compartmentalization of the plasma membrane. Given the ability of the septins to bind GTP and phosphatidylinositol 4,5-bisphosphate in a mutually exclusive manner, these proteins might be crucial elements for the spatial and/or temporal control of diverse cellular functions. As the functions of the septins become unraveled, our understanding of seemingly different cellular processes may move a step further.

scholarly journals Regulation of caveolae through cholesterol-depletion-dependent tubulation mediated by PACSIN2

2020 ◽  
Vol 133 (19) ◽  
pp. jcs246785 ◽  
Author(s):  
Aini Gusmira ◽  
Kazuhiro Takemura ◽  
Shin Yong Lee ◽  
Takehiko Inaba ◽  
Kyoko Hanawa-Suetsugu ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Lipid Composition ◽  
Cholesterol Depletion ◽  
Membrane Deformation ◽  
Bar Domain ◽  
Caveolin 1 ◽  
Membrane Tubulation ◽  
Reconstituted Membranes ◽  
Shaping Ability

ABSTRACTThe membrane-shaping ability of PACSIN2 (also known as syndapin II), which is mediated by its F-BAR domain, has been shown to be essential for caveolar morphogenesis, presumably through the shaping of the caveolar neck. Caveolar membranes contain abundant cholesterol. However, the role of cholesterol in PACSIN2-mediated membrane deformation remains unclear. Here, we show that the binding of PACSIN2 to the membrane can be negatively regulated by cholesterol. We prepared reconstituted membranes based on the lipid composition of caveolae. The reconstituted membrane with cholesterol had a weaker affinity for the F-BAR domain of PACSIN2 than a membrane without cholesterol. Consistent with this, upon depletion of cholesterol from the plasma membrane, PACSIN2 localized at tubules that had caveolin-1 at their tips, suggesting that cholesterol inhibits membrane tubulation mediated by PACSIN2. The tubules induced by PACSIN2 could be representative of an intermediate of caveolae endocytosis. Consistent with this, the removal of caveolae from the plasma membrane upon cholesterol depletion was diminished in the PACSIN2-deficient cells. These data suggest that PACSIN2-mediated caveolae internalization is dependent on the amount of cholesterol, providing a mechanism for cholesterol-dependent regulation of caveolae.This article has an associated First Person interview with the first author of the paper.

scholarly journals New interactions of invadopodia scaffold protein TKS5 with proteins that take part in actin cytoskeleton reorganization, endo-/exocytosis and membrane remodeling

2019 ◽  
Vol 16 (2) ◽  
pp. 183-189
Author(s):  
Y. M. Nemesh ◽  
S. V. Kropyvko
Keyword(s):  
Plasma Membrane ◽  
Actin Cytoskeleton ◽  
Scaffold Protein ◽  
Scaffold Proteins ◽  
Membrane Remodeling ◽  
Sh3 Domains ◽  
Protein Protein Interaction ◽  
Cytoskeleton Reorganization ◽  
New Interactions ◽  
Cytoskeleton Rearrangement

Aim. TKS5 is a key scaffold protein of invadopodia. In its absence, the cells completely lose the ability to form invadopodia. This fact makes TKS5 a potential target for cancer cure and one of the central proteins in the investigation of cancer cell invasion. Additionally, the question remains about the function of TKS5 in normal cells. Therefore, in order to extend knowledge about TKS5 role in healthy and invasive cells, we tested the TKS5 interaction with the proteins involved in signal transduction: PLCγ1, SRC, CRK, CSK; the proteins involved in plasma membrane remodeling: AMPH1, BIN1, CIN85, ITSN1, ITSN2; the protein involved in the actin cytoskeleton rearrangement: CTTN. Methods. We used the GST Pull-down assay to identify the protein-protein interaction. Results. We revealed that TKS5 SH3 domains interact with CIN85. There were identified TKS5 interactions with SH3 domains of CTTN, ITSN1, ITSN2, AMPH1 and BIN1. Conclusions. TKS5 interacts with CIN85, CTTN, ITSN1, ITSN2, AMPH1 and BIN1, which take part in membrane remodeling, endo-/exocytosis and actin cytoskeleton rearrangement. Keywords: TKS5, scaffold proteins, actin cytoskeleton, plasma membrane.

Syndapins, members of the F-BAR subfamily of BAR domain superfamily of proteins, shape the plasma membrane and are crucial for actin cytoskeleton-driven neuromorphogenesis

2009 ◽  
Vol 2009 (Spring) ◽  
Author(s):  
Elavarasi Dharmalingam ◽  
Roser Pinyol ◽  
Akvile Haeckel ◽  
Michael M. Kessels ◽  
Britta Qualmann
Keyword(s):  
Plasma Membrane ◽  
Actin Cytoskeleton ◽  
Bar Domain

scholarly journals Force requirements of endocytic vesicle formation

2020 ◽  
Author(s):  
Marc Abella ◽  
Lynnel Andruck ◽  
Gabriele Malengo ◽  
Michal Skruzny
Keyword(s):  
Plasma Membrane ◽  
Membrane Trafficking ◽  
Turgor Pressure ◽  
Cellular Membrane ◽  
Total Force ◽  
Vesicle Formation ◽  
Endocytic Vesicle ◽  
Bar Domain ◽  
Cellular Processes ◽  
Cell Turgor

AbstractMechanical forces are integral to many cellular processes, including clathrin-mediated endocytosis, a principal membrane trafficking route into the cell. During endocytosis, forces provided by endocytic proteins and the polymerizing actin cytoskeleton reshape the plasma membrane into a vesicle. Assessing force requirements of endocytic membrane remodelling is essential for understanding endocytosis. Here, we determined forces applied during endocytosis using FRET-based tension sensors integrated into the major force-transmitting protein Sla2 in yeast. We measured force of approx. 10 pN transmitted over Sla2 molecule, hence a total force of 450-1300 pN required for endocytic vesicle formation. Importantly, decreasing cell turgor pressure and plasma membrane tension reduced force requirements of endocytosis. The measurements in hypotonic conditions and mutants lacking BAR-domain membrane scaffolds then showed the limits of the endocytic force-transmitting machinery. Our study provides force values and force profiles critical for understanding the mechanics of endocytosis and potentially other key cellular membrane-remodelling processes.

Regulation of the Actin Cytoskeleton-Plasma Membrane Interplay by Phosphoinositides

2010 ◽  
Vol 90 (1) ◽  
pp. 259-289 ◽  
Author(s):  
Juha Saarikangas ◽  
Hongxia Zhao ◽  
Pekka Lappalainen
Keyword(s):  
Plasma Membrane ◽  
Actin Cytoskeleton ◽  
Actin Dynamics ◽  
Actin Binding ◽  
Cell Physiology ◽  
Cortical Actin ◽  
Bar Domain ◽  
Pathogen Invasion ◽  
Associated Proteins ◽  
Continuous Dynamic

The plasma membrane and the underlying cortical actin cytoskeleton undergo continuous dynamic interplay that is responsible for many essential aspects of cell physiology. Polymerization of actin filaments against cellular membranes provides the force for a number of cellular processes such as migration, morphogenesis, and endocytosis. Plasma membrane phosphoinositides (especially phosphatidylinositol bis- and trisphosphates) play a central role in regulating the organization and dynamics of the actin cytoskeleton by acting as platforms for protein recruitment, by triggering signaling cascades, and by directly regulating the activities of actin-binding proteins. Furthermore, a number of actin-associated proteins, such as BAR domain proteins, are capable of directly deforming phosphoinositide-rich membranes to induce plasma membrane protrusions or invaginations. Recent studies have also provided evidence that the actin cytoskeleton-plasma membrane interactions are misregulated in a number of pathological conditions such as cancer and during pathogen invasion. Here, we summarize the wealth of knowledge on how the cortical actin cytoskeleton is regulated by phosphoinositides during various cell biological processes. We also discuss the mechanisms by which interplay between actin dynamics and certain membrane deforming proteins regulate the morphology of the plasma membrane.

scholarly journals Role of MCC/Eisosome in Fungal Lipid Homeostasis

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 305 ◽  
Author(s):  
Zahumensky ◽  
Malinsky
Keyword(s):  
Plasma Membrane ◽  
Lipid Composition ◽  
Molecular Mechanisms ◽  
Membrane Lipid ◽  
Membrane Microdomains ◽  
Bar Domain ◽  
Cellular Processes ◽  
Membrane Microdomain ◽  
Membrane Compartment ◽  
Plasma Membrane Domain

One of the best characterized fungal membrane microdomains is the MCC/eisosome. The MCC (membrane compartment of Can1) is an evolutionarily conserved ergosterol-rich plasma membrane domain. It is stabilized on its cytosolic face by the eisosome, a hemitubular protein complex composed of Bin/Amphiphysin/Rvs (BAR) domain-containing Pil1 and Lsp1. These two proteins bind directly to phosphatidylinositol 4,5-bisphosphate and promote the typical furrow-like shape of the microdomain, with highly curved edges and bottom. While some proteins display stable localization in the MCC/eisosome, others enter or leave it under particular conditions, such as misbalance in membrane lipid composition, changes in membrane tension, or availability of specific nutrients. These findings reveal that the MCC/eisosome, a plasma membrane microdomain with distinct morphology and lipid composition, acts as a multifaceted regulator of various cellular processes including metabolic pathways, cellular morphogenesis, signalling cascades, and mRNA decay. In this minireview, we focus on the MCC/eisosome’s proposed role in the regulation of lipid metabolism. While the molecular mechanisms of the MCC/eisosome function are not completely understood, the idea of intracellular processes being regulated at the plasma membrane, the foremost barrier exposed to environmental challenges, is truly exciting.

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