2 research outputs found
Phosphoinositide-binding interface proteins involved in shaping cell membranes
- Author
- C. Yang M. Hoelzle, A. Disanza, G.
- C.J. Merrifield B. Qualmann, M.M.
- D. Kenney L. Cairns, E. Remold-O
- E.D. Gundelfinger M.M. Kessels and
- F. Kanai H. Liu, S.J. Field, H. Ak
- G. Scita S. Confalonieri, P. Lappa
- J. Saarikangas H. Zhao, A. Pykalai
- K. Hori H. Yasuda, D. Konno, H. Ma
- M.L. Cheever T.K. Sato, T. de Beer
- MODREGGER J
- S. Krugmann I. Jordens, K. Gevaert
- S.L. Blagg M. Stewart, C. Sambles
- T. Itoh and T. Takenawa
- T. Itoh J. Hasegawa, K. Tsujita, Y
- T. Takenawa and T. Itoh
- TAKENAWA TADAOMI
- W.M. Henne H.M. Kent, M.G. Ford, B
- Y. Nishizuka
- Publication venue
- The Japan Academy
- Publication date
- 01/01/2010
- Field of study
The mechanism by which cell and cell membrane shapes are created has long been a subject of great interest. Among the phosphoinositide-binding proteins, a group of proteins that can change the shape of membranes, in addition to the phosphoinositide-binding ability, has been found. These proteins, which contain membrane-deforming domains such as the BAR, EFC/F-BAR, and the IMD/I-BAR domains, led to inward-invaginated tubes or outward protrusions of the membrane, resulting in a variety of membrane shapes. Furthermore, these proteins not only bind to phosphoinositide, but also to the N-WASP/WAVE complex and the actin polymerization machinery, which generates a driving force to shape the membranes
Physical role of nuclear and cytoskeletal confinements in cell migration mode selection and switching
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- Publication venue
- 'American Institute of Mathematical Sciences (AIMS)'
- Publication date
- 01/01/2017
- Field of study