LoboVault Home

Identification of mitogen-activated protein kinase docking sites in enzymes that metabolize phosphatidylinositols and inositol phosphates

LoboVault

Please use this identifier to cite or link to this item: http://hdl.handle.net/1928/6888

Identification of mitogen-activated protein kinase docking sites in enzymes that metabolize phosphatidylinositols and inositol phosphates

Show simple item record

dc.contributor.author Sosa, Marcos
dc.contributor.author Caldwell, Kevin
dc.contributor.author Buckley, Colin
dc.date.accessioned 2008-08-22T18:22:00Z
dc.date.available 2008-08-22T18:22:00Z
dc.date.issued 2008-08-22T18:22:00Z
dc.identifier.uri http://hdl.handle.net/1928/6888
dc.description.abstract Background: Reversible interactions between the components of cellular signaling pathways allow for the formation and dissociation of multimolecular complexes with spatial and temporal resolution and, thus, are an important means of integrating multiple signals into a coordinated cellular response. Several mechanisms that underlie these interactions have been identified, including the recognition of specific docking sites, termed a D-domain and FXFP motif, on proteins that bind mitogen-activated protein kinases (MAPKs). We recently found that phosphatidylinositol-specific phospholipase C-γ1 (PLC-γ1) directly binds to extracellular signal-regulated kinase 2 (ERK2), a MAPK, via a D-domain-dependent mechanism. In addition, we identified D-domain sequences in several other PLC isozymes. In the present studies we sought to determine whether MAPK docking sequences could be recognized in other enzymes that metabolize phosphatidylinositols (PIs), as well as in enzymes that metabolize inositol phosphates (IPs). Results: We found that several, but not all, of these enzymes contain identifiable D-domain sequences. Further, we found a high degree of conservation of these sequences and their location in human and mouse proteins; notable exceptions were PI 3-kinase C2-γ, PI 4-kinase type IIβ, and inositol polyphosphate 1- phosphatase. Conclusion: The results indicate that there may be extensive crosstalk between MAPK signaling and signaling pathways that are regulated by cellular levels of PIs or IPs. en_US
dc.language.iso en_US en_US
dc.subject phosphatidylinositols and inositol phosphates en_US
dc.subject mitogen-activated protein kinase docking sites en_US
dc.title Identification of mitogen-activated protein kinase docking sites in enzymes that metabolize phosphatidylinositols and inositol phosphates en_US
dc.type Article en_US


Files in this item

Files Size Format View
Sosa Final Paper.pdf 692.3Kb PDF View/Open

This item appears in the following Collection(s)

Show simple item record

UNM Libraries

Search LoboVault


Browse

My Account