scholarly journals Lipid rafts serve as signaling platforms for mGlu1 receptor-mediated calcium signaling in association with caveolin

2014 ◽  
Vol 7 (1) ◽  
pp. 9 ◽  
Author(s):  
Seung-Eon Roh ◽  
Yun Hong ◽  
Dong Jang ◽  
Jun Kim ◽  
Sang Kim
Keyword(s):  
Calcium Signaling ◽  
Lipid Rafts ◽  
Mglu1 Receptor

scholarly journals Lipid rafts/caveolae as microdomains of calcium signaling

Cell Calcium ◽  
2009 ◽  
Vol 45 (6) ◽  
pp. 625-633 ◽  
Author(s):  
Biswaranjan Pani ◽  
Brij B. Singh
Keyword(s):  
Calcium Signaling ◽  
Lipid Rafts

scholarly journals Soluble klotho regulates TRPC6 calcium signaling via lipid rafts, independent of the FGFR‐FGF23 pathway

2019 ◽  
Vol 33 (8) ◽  
pp. 9182-9193 ◽  
Author(s):  
Jon D. Wright ◽  
Sung‐Wan An ◽  
Jian Xie ◽  
Carmay Lim ◽  
Chou‐Long Huang
Keyword(s):  
Calcium Signaling ◽  
Lipid Rafts

scholarly journals Cutting Edge: Optical Microspectrophotometry Supports the Existence of Gel Phase Lipid Rafts at the Lamellipodium of Neutrophils: Apparent Role in Calcium Signaling

2004 ◽  
Vol 172 (8) ◽  
pp. 4681-4685 ◽  
Author(s):  
Andrei L. Kindzelskii ◽  
Robert G. Sitrin ◽  
Howard R. Petty
Keyword(s):  
Calcium Signaling ◽  
Lipid Rafts ◽  
Cutting Edge ◽  
Gel Phase

Caveolin-1, galectin-3 and lipid raft domains in cancer cell signalling

2015 ◽  
Vol 57 ◽  
pp. 189-201 ◽  
Author(s):  
Jay Shankar ◽  
Cecile Boscher ◽  
Ivan R. Nabi
Keyword(s):  
Plasma Membrane ◽  
Lipid Rafts ◽  
Cancer Cell ◽  
Cellular Response ◽  
Spatial Organization ◽  
Essential Feature ◽  
Cell Signalling ◽  
Coated Pits ◽  
Signalling Molecules ◽  
Raft Domains

Spatial organization of the plasma membrane is an essential feature of the cellular response to external stimuli. Receptor organization at the cell surface mediates transmission of extracellular stimuli to intracellular signalling molecules and effectors that impact various cellular processes including cell differentiation, metabolism, growth, migration and apoptosis. Membrane domains include morphologically distinct plasma membrane invaginations such as clathrin-coated pits and caveolae, but also less well-defined domains such as lipid rafts and the galectin lattice. In the present chapter, we will discuss interaction between caveolae, lipid rafts and the galectin lattice in the control of cancer cell signalling.

Spatial control of actin-based motility through plasmalemmal PtdIns(4,5)P2-rich raft assemblies.

2005 ◽  
Vol 72 ◽  
pp. 119-127 ◽  
Author(s):  
Tamara Golub ◽  
Caroni Pico
Keyword(s):  
Protein Kinase ◽  
Cell Surface ◽  
Actin Cytoskeleton ◽  
Lipid Rafts ◽  
Patch Clustering ◽  
Pkc Protein Kinase C ◽  
Membrane Bound ◽  
And Function ◽  
Cytoskeleton Dynamics ◽  
Syndrome Protein

The interactions of cells with their environment involve regulated actin-based motility at defined positions along the cell surface. Sphingolipid- and cholesterol-dependent microdomains (rafts) order proteins at biological membranes, and have been implicated in most signalling processes at the cell surface. Many membrane-bound components that regulate actin cytoskeleton dynamics and cell-surface motility associate with PtdIns(4,5)P2-rich lipid rafts. Although raft integrity is not required for substrate-directed cell spreading, or to initiate signalling for motility, it is a prerequisite for sustained and organized motility. Plasmalemmal rafts redistribute rapidly in response to signals, triggering motility. This process involves the removal of rafts from sites that are not interacting with the substrate, apparently through endocytosis, and a local accumulation at sites of integrin-mediated substrate interactions. PtdIns(4,5)P2-rich lipid rafts can assemble into patches in a process depending on PtdIns(4,5)P2, Cdc42 (cell-division control 42), N-WASP (neural Wiskott-Aldrich syndrome protein) and actin cytoskeleton dynamics. The raft patches are sites of signal-induced actin assembly, and their accumulation locally promotes sustained motility. The patches capture microtubules, which promote patch clustering through PKA (protein kinase A), to steer motility. Raft accumulation at the cell surface, and its coupling to motility are influenced greatly by the expression of intrinsic raft-associated components that associate with the cytosolic leaflet of lipid rafts. Among them, GAP43 (growth-associated protein 43)-like proteins interact with PtdIns(4,5)P2 in a Ca2+/calmodulin and PKC (protein kinase C)-regulated manner, and function as intrinsic determinants of motility and anatomical plasticity. Plasmalemmal PtdIns(4,5)P2-rich raft assemblies thus provide powerful organizational principles for tight spatial and temporal control of signalling in motility.

664: CXCL12/CXCR4 Trans-Activation of HER2 in Lipid Rafts of Prostate Cancer Cell Membranes Promotes Bone Metastasis

2007 ◽  
Vol 177 (4S) ◽  
pp. 223-223
Author(s):  
Sreenivasa R. Chinni ◽  
Hamilto Yamamoto ◽  
Zhong Dong ◽  
Aaron Sabbota ◽  
Sanaa Nabha ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Bone Metastasis ◽  
Lipid Rafts ◽  
Cancer Cell ◽  
Cell Membranes ◽  
Prostate Cancer Cell

173: Lipid Rafts are Negative Regulators of TGFβ Signaling in Ureteral Smooth Muscle Cells

2004 ◽  
Vol 171 (4S) ◽  
pp. 46-46
Author(s):  
Carlos R. Estrada ◽  
Theodora Danciu ◽  
Maximilian Stehr ◽  
Joseph Khoury ◽  
Keith R. Solomon ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Lipid Rafts ◽  
Muscle Cells ◽  
Negative Regulators ◽  
Tgfβ Signaling

63 SAP-97 promotes hKv1.5 compartmentation to lipid rafts and interaction with beta-subunit: consequences on currents properties

2003 ◽  
Vol 2 (1) ◽  
pp. 4
Author(s):  
A MAGUY ◽  
D GODREAU ◽  
P RATAJCZAK ◽  
C HEYMES ◽  
R VRANCKX ◽  
...  
Keyword(s):  
Lipid Rafts ◽  
Beta Subunit

Effects of Cyclic Peptide (Pro-Leu-Gly)2 on Calcium Signaling in Isolated Myometrial Cells from Pregnant Rat

2001 ◽  
Vol 89 (5) ◽  
pp. 277-280 ◽  
Author(s):  
Yuji Kaneko ◽  
Hideki Shojo ◽  
Takanori Uchimura
Keyword(s):  
Calcium Signaling ◽  
Cyclic Peptide ◽  
Pregnant Rat ◽  
Myometrial Cells

Calcium signaling explained in new model

2014 ◽  
Author(s):  
Sara Osman
Keyword(s):  
Calcium Signaling ◽  
New Model
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