Title

CPI-17 Likes To Move It Move It!

Poster Number

21

Lead Author Major

Biological Sciences

Format

Poster Presentation

Faculty Mentor Name

Douglas Weiser

Faculty Mentor Department

Biological Sciences

Abstract/Artist Statement

The phosphorylation of myosin II is an important cellular control mechanism for cell migration processes in many organisms. Cell migration is an important process in cell physiology and often times is misregulated in cancer. Phosphorylation of myosin II is regulated by the activity of CPI-17 (C-kinase potentiated protein phosphatase-1 Inhibitor Mr = 17 kDa), which is a protein phosphatase-1 (PP1) inhibitor protein. Myosin phosphatase helps in the relaxation of actin and myosin in the cell. CPI-17 inhibits myosin light chain phosphatase which is comprised of MYPT1 and PP1. Multiple kinases signal through this mechanism, many of which are not fully understood. Much remains to be learned how CPI- 17 affects cell migration. To learn more about CPI-17 we cloned CPI-17 from zebrafish and are researching to observe the role of CPI-17 in embryonic development of zebrafish. The CPI-17 cDNA was amplified using PCR and cloned into a pGEX4T vector to form a bacterial construct, which was verified by sequencing. To further validate the construct protein expression, the protein was purified from the bacterial cells. We are currently working on assembling a mammalian construct with CPI-17, which will allow us to express the protein and understand its affect on cell contraction by using cells to see actin myosin contractility by assaying cell shape.

Location

DeRosa University Center, Ballroom

Start Date

21-4-2011 6:00 PM

End Date

21-4-2011 8:00 PM

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Apr 21st, 6:00 PM Apr 21st, 8:00 PM

CPI-17 Likes To Move It Move It!

DeRosa University Center, Ballroom

The phosphorylation of myosin II is an important cellular control mechanism for cell migration processes in many organisms. Cell migration is an important process in cell physiology and often times is misregulated in cancer. Phosphorylation of myosin II is regulated by the activity of CPI-17 (C-kinase potentiated protein phosphatase-1 Inhibitor Mr = 17 kDa), which is a protein phosphatase-1 (PP1) inhibitor protein. Myosin phosphatase helps in the relaxation of actin and myosin in the cell. CPI-17 inhibits myosin light chain phosphatase which is comprised of MYPT1 and PP1. Multiple kinases signal through this mechanism, many of which are not fully understood. Much remains to be learned how CPI- 17 affects cell migration. To learn more about CPI-17 we cloned CPI-17 from zebrafish and are researching to observe the role of CPI-17 in embryonic development of zebrafish. The CPI-17 cDNA was amplified using PCR and cloned into a pGEX4T vector to form a bacterial construct, which was verified by sequencing. To further validate the construct protein expression, the protein was purified from the bacterial cells. We are currently working on assembling a mammalian construct with CPI-17, which will allow us to express the protein and understand its affect on cell contraction by using cells to see actin myosin contractility by assaying cell shape.