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10.1186/1741-7007-12-43 http://scihub22266oqcxt.onion/10.1186/1741-7007-12-43 C4071339!4071339 !24885555     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 276.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 276.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 276.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 276.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\24885555 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       BMC+Biol 2014 ; 12 (ä): 43 Nephropedia Template TP {{tp|p=24885555 |t=2014. BMP2-induced chemotaxis requires PI3K p55?/p110?-dependent phosphatidylinositol (3,4,5)-triphosphate production and LL5? recruitment at the cytocortex |pdf=|usr=}}{{24885555 }} gab.com Text BMP2-induced chemotaxis requires PI3K p55 /p110 -dependent phosphatidylinositol (3,4,5)-triphosphate production and LL5 recruitment at the cytocortex JO: BMC Biol http://www.kidney.de/pget.php?&tw=1&pmid=24885555 #FOAvip BACKGROUND: BMP-induced chemotaxis of mesenchymal progenitors is fundamental for vertebrate development, disease and tissue repair. BMP2 induces Smad and non-Smad signalling. Whereas signal transduction via Smads lead to transcriptional responses, non-Smad signalling induces both, transcriptional and immediate/early non-transcriptional responses. However, the molecular mechanisms by which BMP2 facilitates planar cell polarity, cortical actin rearrangements, lamellipodia formation and chemotaxis of mesenchymal progenitors are poorly understood. Our aim was to uncover the molecular mechanism by which BMP2 facilitates chemotaxis via the BMP2-dependent activation of PI3K and spatiotemporal control of PIP3 production important for actin rearrangements at the mesenchymal cell cytocortex. RESULTS: We unveiled the molecular mechanism by which BMP2 induces non-Smad signalling by PI3K and the role of the second messenger PIP3 in BMP2-induced planar cell polarity, cortical actin reorganisation and lamellipodia formation. By using protein interaction studies, we identified the class Ia PI3K regulatory subunit p55? to act as a specific and non-redundant binding partner for BMP receptor type II (BMPRII) in concert with the catalytic subunit p110?. We mapped the PI3K interaction to a region within the BMPRII kinase. Either BMP2 stimulation or increasing amounts of BMPRI facilitated p55? association with BMPRII, but BMPRII kinase activity was not required for the interaction. We visualised BMP2-dependent PIP3 production via PI3K p55?/p110? and were able to localise PIP3 to the leading edge of intact cells during the process of BMP2-induced planar cell polarity and actin dependent lamellipodia formation. Using mass spectrometry, we found the highly PIP3-sensitive PH-domain protein LL5? to act as a novel BMP2 effector in orchestrating cortical actin rearrangements. By use of live cell imaging we found that knock-down of p55? or LL5? or pharmacological inhibition of PI3K impaired BMP2-induced migratory responses. CONCLUSIONS: Our results provide evidence for an important contribution of the BMP2-PI3K (p55?/p110?)- PIP3-LL5? signalling axis in mesenchymal progenitor cell chemotaxis. We demonstrate molecular insights into BMP2-induced PI3K signalling on the level of actin reorganisation at the leading edge cytocortex. These findings are important to better understand BMP2-induced cytoskeletal reorganisation and chemotaxis of mesenchymal progenitors in different physiological or pathophysiological contexts. Twit Text FOAVip BMP2-induced chemotaxis requires PI3K p55 /p110 -dependent phosphatidylinositol (3,4,5)-triphosphate production and LL5 recruitment at the cytocortex ????BMC Biol http://www.kidney.de/pget.php?&tw=1&pmid=24885555 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24885555 #FOAvip English Wikipedia <ref>{{Cite pmid|24885555 }}</ref> BMP2-induced chemotaxis requires PI3K p55?/p110?-dependent phosphatidylinositol (3,4,5)-triphosphate production and LL5? recruitment at the cytocortex #MMPMID24885555 Hiepen C ; Benn A ; Denkis A ; Lukonin I ; Weise C ; Boergermann JH ; Knaus P BMC Biol 2014[May]; 12 (ä): 43 PMID24885555 show ga BACKGROUND: BMP-induced chemotaxis of mesenchymal progenitors is fundamental for vertebrate development, disease and tissue repair. BMP2 induces Smad and non-Smad signalling. Whereas signal transduction via Smads lead to transcriptional responses, non-Smad signalling induces both, transcriptional and immediate/early non-transcriptional responses. However, the molecular mechanisms by which BMP2 facilitates planar cell polarity, cortical actin rearrangements, lamellipodia formation and chemotaxis of mesenchymal progenitors are poorly understood. Our aim was to uncover the molecular mechanism by which BMP2 facilitates chemotaxis via the BMP2-dependent activation of PI3K and spatiotemporal control of PIP3 production important for actin rearrangements at the mesenchymal cell cytocortex. RESULTS: We unveiled the molecular mechanism by which BMP2 induces non-Smad signalling by PI3K and the role of the second messenger PIP3 in BMP2-induced planar cell polarity, cortical actin reorganisation and lamellipodia formation. By using protein interaction studies, we identified the class Ia PI3K regulatory subunit p55? to act as a specific and non-redundant binding partner for BMP receptor type II (BMPRII) in concert with the catalytic subunit p110?. We mapped the PI3K interaction to a region within the BMPRII kinase. Either BMP2 stimulation or increasing amounts of BMPRI facilitated p55? association with BMPRII, but BMPRII kinase activity was not required for the interaction. We visualised BMP2-dependent PIP3 production via PI3K p55?/p110? and were able to localise PIP3 to the leading edge of intact cells during the process of BMP2-induced planar cell polarity and actin dependent lamellipodia formation. Using mass spectrometry, we found the highly PIP3-sensitive PH-domain protein LL5? to act as a novel BMP2 effector in orchestrating cortical actin rearrangements. By use of live cell imaging we found that knock-down of p55? or LL5? or pharmacological inhibition of PI3K impaired BMP2-induced migratory responses. CONCLUSIONS: Our results provide evidence for an important contribution of the BMP2-PI3K (p55?/p110?)- PIP3-LL5? signalling axis in mesenchymal progenitor cell chemotaxis. We demonstrate molecular insights into BMP2-induced PI3K signalling on the level of actin reorganisation at the leading edge cytocortex. These findings are important to better understand BMP2-induced cytoskeletal reorganisation and chemotaxis of mesenchymal progenitors in different physiological or pathophysiological contexts. |Actins/metabolism [MESH] |Amino Acid Sequence [MESH] |Androstadienes/pharmacology [MESH] |Animals [MESH] |Bone Morphogenetic Protein 2/*pharmacology [MESH] |Bone Morphogenetic Protein Receptors, Type I [MESH] |Bone Morphogenetic Protein Receptors, Type II/metabolism [MESH] |Carrier Proteins/*metabolism [MESH] |Cell Line [MESH] |Chemotaxis/*drug effects [MESH] |Class Ia Phosphatidylinositol 3-Kinase/chemistry/*metabolism [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Inositol Phosphates/*biosynthesis [MESH] |Membrane Proteins/*metabolism [MESH] |Mesoderm/cytology [MESH] |Mice [MESH] |Microfilament Proteins/*metabolism [MESH] |Models, Biological [MESH] |Molecular Sequence Data [MESH] |Myoblasts/*cytology/drug effects/*enzymology/metabolism [MESH] |Peptides/chemistry [MESH] |Phosphorylation/drug effects [MESH] |Phosphotyrosine/metabolism [MESH] |Protein Binding/drug effects [MESH] |Pseudopodia/drug effects/metabolism [MESH] |Signal Transduction/drug effects [MESH]BMP2-induced chemotaxis requires PI3K p55?/p110?-dependent phosphatidy(epmc).pdf DeepDyve Pubget Overpricing