End-binding protein

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End-binding protein or telomere-binding protein or microtubule-associated protein RP/EB family member (EB) regulates microtubules dynamics, promotes colony formation and enhances tumor growth. EB is part of the proteins which accumulate at the growing microtubule plus end. During mitosis the EB associates with centrosome and spindle microtubules. EB is involved in the regulation of chromosome stability and microtubule structure. The C terminal domains of EB1 and EB3 are involved in dimer formation. The CH (Calponin Homology) domain is an actin-binding domain[1].

  • End-binding protein 1 accumulates at growing microtubule ends and regulates their dynamics[2].
  • End-binding protein 2 is involved in initial microtubule reorganization promoting stability and bundle formation[3].


Human end-binding protein 1 C terminal (grey) complex with dynactin-1 CAP-GLY domain (green) (PDB code 2hkq)

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3D Structures of end-binding protein

Updated on 16-June-2024

References

  1. Nakamura M, Zhou XZ, Lu KP. Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization. Curr Biol. 2001 Jul 10;11(13):1062-7. PMID:11470413
  2. Nehlig A, Molina A, Rodrigues-Ferreira S, Honoré S, Nahmias C. Regulation of end-binding protein EB1 in the control of microtubule dynamics. Cell Mol Life Sci. 2017 Jul;74(13):2381-2393. PMID:28204846 doi:10.1007/s00018-017-2476-2
  3. Goldspink DA, Gadsby JR, Bellett G, Keynton J, Tyrrell BJ, Lund EK, Powell PP, Thomas P, Mogensen MM. The microtubule end-binding protein EB2 is a central regulator of microtubule reorganisation in apico-basal epithelial differentiation. J Cell Sci. 2013 Sep 1;126(Pt 17):4000-14. PMID:23813963 doi:10.1242/jcs.129759

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