Due to a temporary embargo, Chapter 6 and Appendix B cannot yet be made available at RePub.
Abstract
Due to a temporary embargo, Chapter 6 and Appendix B cannot yet be made available at RePub.Microtubules are a part of the
cytoskeleton involved in many essential processes, such
as intracellular transport of cargoes, cell migration,
positioning of cellular organelles and formation of the
mitotic spindle for chromosome segregation. The fast
growing end of microtubules (the plus-end) can interact
with specific microtubule plus-end binding proteins
(also known as plus-end tracking proteins, or +TIPs).
+TIPs participate in microtubule interactions with
different cellular structures and control microtubule
dynamics. This thesis describes the functional analysis
of protein interactions at the microtubule plus-ends.
The microtubule plus-end tracking protein CLIP-170
(cytoplasmic linker protein of 170 kDa) regulates its
association with microtubules by changing its
conformation. The folded head-to-tail conformation of
CLIP-170 inhibits microtubule association and also
interferes with the binding of dynactin and LIS1 to the
CLIP-170 COOH terminus.
The functional relationship of CLIP family members with
three EB family members EB1, EB2 and EB3 is described.
CLIPs bind directly to the COOH terminus of the E
