scholarly journals Role of Phosphoinositides in Cellular Signaling, Functions and Diseases

2020 ◽  
Author(s):  
Kalpana Mandal
Keyword(s):  
Cell Signaling ◽  
Transmembrane Proteins ◽  
Adaptor Proteins ◽  
Membrane Curvature ◽  
Membrane Dynamics ◽  
Actin Binding ◽  
Coated Pits ◽  
Cytoskeletal Dynamics ◽  
Actin Cytoskeletal Dynamics

In this review we summarize the recent development in understanding the role of PIP2 in cellular function and signaling. We first discuss the effect of PIP2 on actin binding proteins addressing the mechanism of the actin cytoskeletal dynamics such as polymerization or depolymerization of the filamentous network or the coupling to membrane to generate forces. Next, we outline the role of PIP2 in membrane dynamics. We summarized how the membrane organization depends upon PIP2 in the presence of ions or transmembrane proteins that are sensitive to membrane curvature. We discuss how clathrin coated pits interact with adaptor proteins during the endocytosis process, which is facilitated by PIP2. Finally, we discuss the role of PIP2 in cell signaling and diseases.

Role of actin-binding proteins in cytoskeletal dynamics

1991 ◽  
Vol 19 (4) ◽  
pp. 1016-1020 ◽  
Author(s):  
A. G. Weeds ◽  
J. Gooch ◽  
M. Hawkins ◽  
B. Pope ◽  
M. Way
Keyword(s):  
Binding Proteins ◽  
Actin Binding ◽  
Actin Binding Proteins ◽  
Cytoskeletal Dynamics

scholarly journals Role of Cyclic Nucleotide-Dependent Actin Cytoskeletal Dynamics: [Ca2+]i and Force Suppression in Forskolin-Pretreated Porcine Coronary Arteries

PLoS ONE ◽  
2013 ◽  
Vol 8 (4) ◽  
pp. e60986 ◽  
Author(s):  
Kyle M. Hocking ◽  
Franz J. Baudenbacher ◽  
Gowthami Putumbaka ◽  
Sneha Venkatraman ◽  
Joyce Cheung-Flynn ◽  
...  
Keyword(s):  
Coronary Arteries ◽  
Cyclic Nucleotide ◽  
Cytoskeletal Dynamics ◽  
Actin Cytoskeletal Dynamics

scholarly journals Toll-Like Receptor Signaling Pathways—Therapeutic Opportunities

2010 ◽  
Vol 2010 ◽  
pp. 1-7 ◽  
Author(s):  
Jiankun Zhu ◽  
Chandra Mohan
Keyword(s):  
Infectious Disease ◽  
Signaling Pathways ◽  
Transmembrane Proteins ◽  
Adaptor Proteins ◽  
Protective Role ◽  
Toll Like Receptor ◽  
Tlr Signaling ◽  
Inflammatory Genes ◽  
The Impact

Toll-like receptors (TLRs) are transmembrane proteins acting mainly as sensors of microbial components. Triggering TLRs results in increased expression of multiple inflammatory genes, which then play a protective role against infection. However, aberrant activation of TLR signaling has a significant impact on the onset of cancer, allergy, sepsis and autoimmunity. Various adaptor proteins, including MyD88, IRAKs, TIRAP, TRIF, and TRAM, are involved in specific TLR signaling pathways. This article reviews the role of these molecules in TLR signaling, and discusses the impact of this pathway on various disease scenarios. Given their important role in infectious and non-infectious disease settings, TLRs and their signaling pathways emerge as attractive targets for therapeutics.

scholarly journals Missing-in-metastasis and IRSp53 deform PI(4,5)P2-rich membranes by an inverse BAR domain–like mechanism

2007 ◽  
Vol 176 (7) ◽  
pp. 953-964 ◽  
Author(s):  
Pieta K. Mattila ◽  
Anette Pykäläinen ◽  
Juha Saarikangas ◽  
Ville O. Paavilainen ◽  
Helena Vihinen ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Membrane Curvature ◽  
Membrane Dynamics ◽  
Actin Dynamics ◽  
Actin Binding ◽  
Tubular Structures ◽  
Membrane Deformation ◽  
Bar Domain ◽  
Membrane Protrusions ◽  
Induce Plasma

The actin cytoskeleton plays a fundamental role in various motile and morphogenetic processes involving membrane dynamics. We show that actin-binding proteins MIM (missing-in-metastasis) and IRSp53 directly bind PI(4,5)P2-rich membranes and deform them into tubular structures. This activity resides in the N-terminal IRSp53/MIM domain (IMD) of these proteins, which is structurally related to membrane-tubulating BAR (Bin/amphiphysin/Rvs) domains. We found that because of a difference in the geometry of the PI(4,5)P2-binding site, IMDs induce a membrane curvature opposite that of BAR domains and deform membranes by binding to the interior of the tubule. This explains why IMD proteins induce plasma membrane protrusions rather than invaginations. We also provide evidence that the membrane-deforming activity of IMDs, instead of the previously proposed F-actin–bundling or GTPase-binding activities, is critical for the induction of the filopodia/microspikes in cultured mammalian cells. Together, these data reveal that interplay between actin dynamics and a novel membrane-deformation activity promotes cell motility and morphogenesis.

scholarly journals Cofilin Phosphorylation and Actin Cytoskeletal Dynamics Regulated by Rho- and Cdc42-Activated Lim-Kinase 2

1999 ◽  
Vol 147 (7) ◽  
pp. 1519-1532 ◽  
Author(s):  
Tomoyuki Sumi ◽  
Kunio Matsumoto ◽  
Yoshimi Takai ◽  
Toshikazu Nakamura
Keyword(s):  
Actin Filaments ◽  
Stress Fibers ◽  
Actin Binding ◽  
Cytoskeletal Reorganization ◽  
Lim Kinase ◽  
Cofilin Phosphorylation ◽  
Induced Stress ◽  
Cytoskeletal Dynamics ◽  
Actin Cytoskeletal Dynamics ◽  
Lamellipodia Formation

The rapid turnover of actin filaments and the tertiary meshwork formation are regulated by a variety of actin-binding proteins. Protein phosphorylation of cofilin, an actin-binding protein that depolymerizes actin filaments, suppresses its function. Thus, cofilin is a terminal effector of signaling cascades that evokes actin cytoskeletal rearrangement. When wild-type LIMK2 and kinase-dead LIMK2 (LIMK2/KD) were respectively expressed in cells, LIMK2, but not LIMK2/KD, phosphorylated cofilin and induced formation of stress fibers and focal complexes. LIMK2 activity toward cofilin phosphorylation was stimulated by coexpression of activated Rho and Cdc42, but not Rac. Importantly, expression of activated Rho and Cdc42, respectively, induced stress fibers and filopodia, whereas both Rho- induced stress fibers and Cdc42-induced filopodia were abrogated by the coexpression of LIMK2/KD. In contrast, the coexpression of LIMK2/KD with the activated Rac did not affect Rac-induced lamellipodia formation. These results indicate that LIMK2 plays a crucial role both in Rho- and Cdc42-induced actin cytoskeletal reorganization, at least in part by inhibiting the functions of cofilin. Together with recent findings that LIMK1 participates in Rac-induced lamellipodia formation, LIMK1 and LIMK2 function under control of distinct Rho subfamily GTPases and are essential regulators in the Rho subfamilies-induced actin cytoskeletal reorganization.

Clathrin Hub Expression Dissociates the Actin-Binding Protein Hip1R from Coated Pits and Disrupts Their Alignment with the Actin Cytoskeleton

Traffic ◽  
2001 ◽  
Vol 2 (11) ◽  
pp. 851-858 ◽  
Author(s):  
Elizabeth M. Bennett ◽  
Chih-Ying Chen ◽  
Asa E. Y. Engqvist-Goldstein ◽  
David G. Drubin ◽  
Frances M. Brodsky
Keyword(s):  
Actin Cytoskeleton ◽  
Binding Protein ◽  
Actin Binding ◽  
Coated Pits ◽  
Actin Binding Protein
Sign in / Sign up

Export Citation Format

Share Document