Asset Details
Do you wish to reserve the book?
A double point mutation in PCL- gamma 1 (Y509A/F510A) enhances Y783 phosphorylation and inositol phospholipid-hydrolyzing activity upon EGF stimulation
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
A double point mutation in PCL- gamma 1 (Y509A/F510A) enhances Y783 phosphorylation and inositol phospholipid-hydrolyzing activity upon EGF stimulation
Do you wish to request the book?
A double point mutation in PCL- gamma 1 (Y509A/F510A) enhances Y783 phosphorylation and inositol phospholipid-hydrolyzing activity upon EGF stimulation
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
A double point mutation in PCL- gamma 1 (Y509A/F510A) enhances Y783 phosphorylation and inositol phospholipid-hydrolyzing activity upon EGF stimulation
2010
Overview
Growth factor stimulation induces Y783 phosphorylation of phosphoinositide-specific PLC- gamma 1, and the subsequent activation of this enzyme in a cellular signaling cascade. Previously, we showed that a double point mutation, Y509A/F510A, of PLC- gamma 1, abolished interactions with translational elongation factor 1- alpha . Here, we report that the Y509A/F510A mutant PLC- gamma 1 displayed extremely high levels of Y783 phosphorylation and enhanced catalytic activity, compared to wild-type PLC- gamma 1, upon treatment of COS7 cells with EGF. In quiescent COS7 cells, the Y509A/F510A mutant PLC- gamma 1 exhibited a constitutive hydrolytic activity, whereas the wild-type counterpart displayed a basal level of activity. Upon treatment of COS7 cells with EGF, the Y783F mutation in Y509A/F510A PLC- gamma 1 (Y509A/F510A/Y783F triple mutant) cells also led to an enhanced catalytic activity, whereas Y783F mutation alone displayed a basal level of activity. Our results collectively suggest that the Y509A/F510A mutant is more susceptible to receptor tyrosine kinase-induced Y783 phosphorylation than is wild-type PLC- gamma 1, but no longer requires Y783 phosphorylation step for the Y509A/F510A mutant PLC- gamma 1 activation in vivo.
We currently cannot retrieve any items related to this title. Kindly check back at a later time.