糖心原创

Contact

• workRoom D116 Medical School
  Queen's Medical Centre
  Nottingham
  NG7 2UH
  UK
• work00 44 115 82 30138
• Claire.Friel@nottingham.ac.uk

Teaching Summary

LIFE2077 (Structure and Function of Proteins), Y2, module convenor

LIFE3092 (The Dynamic Cell), Y3 module convenor

LIFE2073 (Macromolecular Systems), Y2, module contributor

Y3 BSc and Y4 MSci project supervisor (Biochemistry)

Research Summary

Cytoskeletal Dynamics and the Mechanochemistry of Motor Proteins

The major interest of my lab is the role of the kinesin family of motor proteins in controlling cytoskeletal dynamics. Kinesins are crucial engines of eukaryotic self-organisation. Members of the kinesin super-family interact with the microtubule cytoskeleton and play a vital role in transport of cellular cargo and in cell division.

Microtubules are long slender polymers of the protein tubulin. The microtubule cytoskeleton serves as rails for intracellular transport, plays an essential role in positioning and movement of cellular organelles and forms the mitotic spindle which separates sister chromosomes during cell division. The organisation and dynamics of the microtubule cytoskeleton are controlled by accessory proteins, such as the kinesin super-family. Kinesins are motor proteins that hydrolyse ATP to bring about conformational changes within the characteristic motor domain and thereby alter the strength of the kinesin-microtubule interaction. The majority of kinesins translocate along the microtubule using the nucleotide-dependent cycle of binding and detachment to transport cellular cargo. However, one class of kinesins (kinesin-13) does not translocate, but instead diffuses to the end of the microtubule where it binds and depolymerises the microtubule substrate. Microtubule depolymerases are crucial during mitosis, being involved in generating the force required to separate sister chromatids and also in ensuring the correct segregation of chromosomes by correcting inappropriate kinetochore-microtubule attachments.

Work in my lab is currently focused on the molecular mechanisms of microtubule depolymerising kinesins; using as a model the Mitotic Centromere-Associated Kinesin (MCAK), which plays a crucial role in cell division.

Selected Publications

• BELSHAM, HANNAH R. and FRIEL, CLAIRE T., 2019. CYTOSKELETON. 76(7-8), 440-446
• QU Y, HAHN I, LEES M, PARKIN J, VOELZMANN A, DOREY K, RATHBONE A, FRIEL CT, ALLAN VJ, OKENVE-RAMOS P, SANCHEZ-SORIANO N and PROKOP A, 2019. eLife. 8,
• BELSHAM HR and FRIEL CT, 2017. PeerJ. 5, e4034
• PATEL JT, BELSHAM HR, RATHBONE AJ, WICKSTEAD B, GELL C and FRIEL CT, 2016. Open biology. 6(10),

• View all publications

• BELSHAM, HANNAH R. and FRIEL, CLAIRE T., 2019. CYTOSKELETON. 76(7-8), 440-446
• QU Y, HAHN I, LEES M, PARKIN J, VOELZMANN A, DOREY K, RATHBONE A, FRIEL CT, ALLAN VJ, OKENVE-RAMOS P, SANCHEZ-SORIANO N and PROKOP A, 2019. eLife. 8,
• FRIEL CT and WELBURN JP, 2018. Biochemical Society transactions. 46(6), 1665-1672
• BELSHAM HR and FRIEL CT, 2017. PeerJ. 5, e4034
• PATEL JT, BELSHAM HR, RATHBONE AJ, WICKSTEAD B, GELL C and FRIEL CT, 2016. Open biology. 6(10),
• PATEL JT, BELSHAM HR, RATHBONE AJ and FRIEL CT, 2014. Journal of visualized experiments : JoVE.
• SANHAJI M, RITTER A, BELSHAM HR, FRIEL CT, ROTH S, LOUWEN F and YUAN J, 2014. Oncotarget. 5(10), 3130-44
• MOURAD SANHAJI, CLAIRE T FRIEL, LINDA WORDEMAN, FRANK LOUWEN and JUPING YUAN, 2012. Mitotic centromere-associated kinesin (MCAK): a potential cancer drug target. Oncotarget. 2, 935-947
• FRIEL, CLAIRE T. and HOWARD, JONATHON, 2012. Journal of Muscle Research and Cell Motility.
• FRIEL, CLAIRE T, BAGSHAW, CLIVE R and HOWARD, JONATHON, 2011. Methods in Molecular Biology. 777, 177-92
• GELL, CHRISTOPHER, FRIEL, CLAIRE T, BORGONOVO, BARBARA, DRECHSEL, DAVID N, HYMAN, ANTHONY A and HOWARD, JONATHON, 2011. Methods in Molecular Biology. 777, 15-28
• FRIEL, C.T. and HOWARD, J., 2011. EMBO Journal. 30(19), 3928-3939
• CHEN, M.M., BARTLETT, A.I., NERENBERG, P.S., FRIEL, C.T., HACKENBERGER, C.P.R., STULTZ, C.M., RADFORD, S.E. and IMPERIALI, B., 2010. Proceedings of the National Academy of Sciences of the United States of America. 107(52), 22528-22533
• GELL, CHRISTOPHER, BORMUTH, VOLKER, BROUHARD, GARY J, COHEN, DANIEL N, DIEZ, STEFAN, FRIEL, CLAIRE T, HELENIUS, JONNE, NITZSCHE, BERT, PETZOLD, HEIKE, RIBBE, JAN, SCH脛FFER, ERIK and STEAR, JEFFREY H, 2010. Methods in Cell Biology. 95, 221-45
• SANHAJI, M., FRIEL, C.T., KREIS, N.-N., KR脛MER, A., MARTIN, C., HOWARD, J., STREBHARDT, K. and YUAN, J.P., 2010. Molecular and Cellular Biology. 30(11), 2594-2607
• FRIEL, C.T., SMITH, D.A., VENDRUSCOLO, M., GSPONER, J. and RADFORD, S.E., 2009. Nature Structural & Molecular Biology. 16(3), 318-324
• MORTON, VICTORIA L, FRIEL, CLAIRE T, ALLEN, LUCY R, PACI, EMANUELE and RADFORD, SHEENA E, 2007. Journal of Molecular Biology. 371(2), 554-68
• MASCA, S.I, RODRIGUEZ-MENDIETA, I.R, FRIEL, C.T, RADFORD, S.E and SMITH, D.A., 2006. Review of Scientific Instruments. 77, 055105
• HACKENBERGER, C.P.R, FRIEL, C.T and RADFORD, S.E. AND IMPERIALI, B., 2005. Journal of the American Chemical Society. 127, 12882-12889
• CRANZ-MILEVA, S, FRIEL, CT and RADFORD, SE, 2005. Protein Engineering Design & Selection. 18(1), 41-50
• MAXWELL, KL, WILDES, D, ZARRINE-AFSAR, A, DE LOS RIOS, MA, BROWN, AG, FRIEL, CT, HEDBERG, L, HORNG, JC, BONA, D, MILLER, EJ, VALLEE-BELISLE, A, MAIN, ERG, BEMPORAD, F, QIU, LL, TEILUM, K, VU, ND, EDWARDS, AM, RUCZINSKI, I, POULSEN, FM, KRAGELUND, BB, MICHNICK, SW, CHITI, F, BAI, YW, HAGEN, SJ, SERRANO, L, OLIVEBERG, M, RALEIGH, DP, WITTUNG-STAFSHEDE, P, RADFORD, SE, JACKSON, SE, SOSNICK, TR, MARQUSEE, S, DAVIDSON, AR and PLAXCO, KW, 2005. Protein Science. 14(3), 602-616
• PACI, E, FRIEL, C.T, LINDORFF-LARSEN, K, RADFORD, S.E and KARPLUS, M. & VENDRUSCOLO, M., 2004. Proteins: Structure, Function and Genetics. 54, 513-525
• FRIEL, CT, BEDDARD, GS and RADFORD, SE, 2004. Journal Of Molecular Biology. 342(1), 261-273
• FRIEL, CT, CAPALDI, AP and RADFORD, SE, 2003. Journal Of Molecular Biology. 326(1), 293-305