Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P05230 and P21579 Pubmed SVM Score :0.0
Human acidic fibroblast growth factor ( hFGF 1 ) is a potent mitogen and is involved in the regulation of key cellular process such as angiogenesis , differentiation , and morphogenesis . hFGF 1 is a signal peptide less protein that is released into the extracellular compartment as a multiprotein complex consisting of S100A13 , synaptotagmin ( Syt 1 ) , and a hFGF 1 homodimer . ^^^
Interacting proteins: P05230 and P21579 Pubmed SVM Score :0.0
By using p 65 synaptotagmin 1 and fibroblast growth factor ( FGF ) 1 : beta galactosidase ( beta gal ) NIH 3T3 cell co transfectants , we demonstrate that a proteolytic fragment consisting of the extravesicular domain of synaptotagmin 1 is released into the extracellular compartment in response to temperature stress with similar kinetics and pharmacological properties as FGF 1 : beta gal . ^^^ Using a deletion mutant that lacks 95 amino acids from the extravesicular domain of synaptotagmin 1 , neither synaptotagmin 1 nor FGF 1 : beta gal are able to access the stress induced release pathway . ^^^ These data demonstrate that the p 40 fragment derived from synaptotagmin 1 is able to utilize the FGF 1 non classical exocytotic pathway and that the release of FGF 1 is dependent on synaptotagmin 1 . . ^^^
Interacting proteins: P05230 and P21579 Pubmed SVM Score :0.0
However , unlike the FGF 1 release pathway , the IL1alpha release pathway appears to function independently of synaptotagmin ( Syt ) 1 because the expression of a dominant negative form of Syt 1 , which represses the release of FGF 1 , did not inhibit the release of mIL1alpha in response to temperature stress . ^^^
Interacting proteins: P05230 and P21579 Pubmed SVM Score :0.0
The signal peptide less FGF gene family prototype , FGF 1 is released in response to temperature stress in vitro as a latent reducing agent sensitive homodimer non covalently complexed with the extravesicular p 40 domain of p 65 synaptotagmin ( Syt ) 1 . ^^^
Interacting proteins: P05230 and P21579 Pubmed SVM Score :0.0
Although biochemical evidence suggests that the formation of a multiprotein complex containing S100A13 and Synaptotagmin ( Syt ) 1 is important for the release of FGF 1 , it is unclear where this intracellular complex is assembled . ^^^ As a result , we employed real time analysis using confocal fluorescence microscopy to study the spatio temporal aspects of this nonclassical export pathway and demonstrate that heat shock stimulates the redistribution of FGF 1 from a diffuse cytosolic pattern to a locale near the inner surface of the plasma membrane where it colocalized with S100A13 and Syt 1 . ^^^ In addition , coexpression of dominant negative mutant forms of S100A13 and Syt 1 , which both repress the release of FGF 1 , failed to inhibit the stress induced peripheral redistribution of intracellular FGF 1 . ^^^
Interacting proteins: P05230 and P21579 Pubmed SVM Score :0.0
The alternative translation of synaptotagmin 1 mediates the non classical release of FGF 1 . ^^^ Although the extravesicular p 40 domain of the transmembrane protein , p 65 synaptotagmin ( Syt ) 1 , is essential for the non classical export of the signal peptide less structure , FGF 1 , it was not possible to identify a specific intracellular protease responsible for the processing of p 65 Syt1 . ^^^
Interacting proteins: P05230 and P21579 Pubmed SVM Score :0.0
Release of FGF 1 and p 40 synaptotagmin 1 correlates with their membrane destabilizing ability . ^^^
Interacting proteins: P05230 and P21579 Pubmed SVM Score :0.0
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Interacting proteins: P05230 and P21579 Pubmed SVM Score :0.0
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