Show simple item record

dc.contributor.authorSosa, Marcos
dc.contributor.authorCaldwell, Kevin
dc.contributor.authorBuckley, Colin
dc.date.accessioned2008-08-22T18:22:00Z
dc.date.available2008-08-22T18:22:00Z
dc.date.issued2008-08-22T18:22:00Z
dc.identifier.urihttp://hdl.handle.net/1928/6888
dc.description.abstractBackground: 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.isoen_USen_US
dc.subjectphosphatidylinositols and inositol phosphatesen_US
dc.subjectmitogen-activated protein kinase docking sitesen_US
dc.titleIdentification of mitogen-activated protein kinase docking sites in enzymes that metabolize phosphatidylinositols and inositol phosphatesen_US
dc.typeArticleen_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record