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10.1083/jcb.201411024 http://scihub22266oqcxt.onion/10.1083/jcb.201411024 C4460154!4460154 !26056142     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 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\26056142 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Cell+Biol 2015 ; 209 (5 ): 739-57 Nephropedia Template TP {{tp|p=26056142 |t=2015. Secreted HHIP1 interacts with heparan sulfate and regulates Hedgehog ligand localization and function |pdf=|usr=}}{{26056142 }} gab.com Text Secreted HHIP1 interacts with heparan sulfate and regulates Hedgehog ligand localization and function JO: J Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=26056142 #FOAvip Vertebrate Hedgehog (HH) signaling is controlled by several ligand-binding antagonists including Patched-1 (PTCH1), PTCH2, and HH-interacting protein 1 (HHIP1), whose collective action is essential for proper HH pathway activity. However, the molecular mechanisms used by these inhibitors remain poorly understood. In this paper, we investigated the mechanisms underlying HHIP1 antagonism of HH signaling. Strikingly, we found evidence that HHIP1 non-cell-autonomously inhibits HH-dependent neural progenitor patterning and proliferation. Furthermore, this non-cell-autonomous antagonism of HH signaling results from the secretion of HHIP1 that is modulated by cell type-specific interactions with heparan sulfate (HS). These interactions are mediated by an HS-binding motif in the cysteine-rich domain of HHIP1 that is required for its localization to the neuroepithelial basement membrane (BM) to effectively antagonize HH pathway function. Our data also suggest that endogenous, secreted HHIP1 localization to HS-containing BMs regulates HH ligand distribution. Overall, the secreted activity of HHIP1 represents a novel mechanism to regulate HH ligand localization and function during embryogenesis. Twit Text FOAVip Secreted HHIP1 interacts with heparan sulfate and regulates Hedgehog ligand localization and function ????J Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=26056142 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26056142 #FOAvip English Wikipedia <ref>{{Cite pmid|26056142 }}</ref> Secreted HHIP1 interacts with heparan sulfate and regulates Hedgehog ligand localization and function #MMPMID26056142 Holtz AM ; Griffiths SC ; Davis SJ ; Bishop B ; Siebold C ; Allen BL J Cell Biol 2015[Jun]; 209 (5 ): 739-57 PMID26056142 show ga Vertebrate Hedgehog (HH) signaling is controlled by several ligand-binding antagonists including Patched-1 (PTCH1), PTCH2, and HH-interacting protein 1 (HHIP1), whose collective action is essential for proper HH pathway activity. However, the molecular mechanisms used by these inhibitors remain poorly understood. In this paper, we investigated the mechanisms underlying HHIP1 antagonism of HH signaling. Strikingly, we found evidence that HHIP1 non-cell-autonomously inhibits HH-dependent neural progenitor patterning and proliferation. Furthermore, this non-cell-autonomous antagonism of HH signaling results from the secretion of HHIP1 that is modulated by cell type-specific interactions with heparan sulfate (HS). These interactions are mediated by an HS-binding motif in the cysteine-rich domain of HHIP1 that is required for its localization to the neuroepithelial basement membrane (BM) to effectively antagonize HH pathway function. Our data also suggest that endogenous, secreted HHIP1 localization to HS-containing BMs regulates HH ligand distribution. Overall, the secreted activity of HHIP1 represents a novel mechanism to regulate HH ligand localization and function during embryogenesis. |Animals [MESH] |Avian Proteins/genetics/*metabolism [MESH] |Body Patterning/*physiology [MESH] |Carrier Proteins/genetics/*metabolism [MESH] |Chick Embryo [MESH] |Chickens [MESH] |Hedgehog Proteins/genetics/*metabolism [MESH] |Heparitin Sulfate/genetics/*metabolism [MESH] |Neural Stem Cells/cytology/metabolism [MESH]Secreted HHIP1 interacts with heparan sulfate and regulates Hedgehog l(epmc).pdf DeepDyve Pubget Overpricing