Title

Protein Phosphatase 1 RVXF Motif Affiliation with Phactr Protein Binding Ability

Poster Number

40

Lead Author Major

Biological Sciences

Format

Poster Presentation

Faculty Mentor Name

Doug Weiser

Faculty Mentor Department

Biological Sciences

Abstract/Artist Statement

Protein phosphatase1, PP1, is a critical serine threonine phosphatase in eukaryotic cells that controls many physiological processes including cell cycle, metabolism, cell motility, and signaling. PP1â?Ts activity is controlled by specific interactions with a large number of different regulatory subunits, including growth arrest and DNA damage-inducible protein, GADD34, as well as myosin phosphatase target subunit1, MYPT1. A recently discovered and not fully characterized set of these regulatory subunits is the phosphatase and actin regulator, Phactr family. The roles of individual Phactr proteins are not well understood, though Phactr proteins are known to interact with actin in the cytoskeleton and PP1, and they are important in controlling cancer motility, cell motility, and apoptosis. Though they have unconventional PP1 binding domain, the mechanisms by which they do so is unusual. We have taken PP1α and PP1β and performed site-directed mutagenesis in the canonical way to which they bind to their targets. We have also ligated Phactr into vectors to see if it interacts with PP1 in a classical or novel way by using Co-imunoprecipitation, Co-IP, from mammalian cell culture.

Location

DeRosa University Center, Ballroom

Start Date

26-4-2014 2:00 PM

End Date

26-4-2014 4:00 PM

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Apr 26th, 2:00 PM Apr 26th, 4:00 PM

Protein Phosphatase 1 RVXF Motif Affiliation with Phactr Protein Binding Ability

DeRosa University Center, Ballroom

Protein phosphatase1, PP1, is a critical serine threonine phosphatase in eukaryotic cells that controls many physiological processes including cell cycle, metabolism, cell motility, and signaling. PP1â?Ts activity is controlled by specific interactions with a large number of different regulatory subunits, including growth arrest and DNA damage-inducible protein, GADD34, as well as myosin phosphatase target subunit1, MYPT1. A recently discovered and not fully characterized set of these regulatory subunits is the phosphatase and actin regulator, Phactr family. The roles of individual Phactr proteins are not well understood, though Phactr proteins are known to interact with actin in the cytoskeleton and PP1, and they are important in controlling cancer motility, cell motility, and apoptosis. Though they have unconventional PP1 binding domain, the mechanisms by which they do so is unusual. We have taken PP1α and PP1β and performed site-directed mutagenesis in the canonical way to which they bind to their targets. We have also ligated Phactr into vectors to see if it interacts with PP1 in a classical or novel way by using Co-imunoprecipitation, Co-IP, from mammalian cell culture.