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PROSITE documentation PDOC51230 [for PROSITE entry PS51230]

EB1-like C-terminal (EB1-C) domain profile





Description

A group of microtubule-associated proteins called +TIPs (plus end tracking proteins), including EB1 (end-binding protein 1) family proteins, label growing microtubules ends specifically in diverse organisms and are implicated in spindle dynamics, chromosome segregation, and directing microtubules toward cortical sites. EB1 members have a bipartite composition: the N-terminal CH domain (see <PDOC50021>) mediates microtubule plus end localization and a C-terminal cargo binding domain (EB1-C) that captures cell polarity determinants. The EB1-C domain comprises a unique EB1-like sequence motif that acts as a binding site for other +TIP proteins. It interacts with the carboxy terminus of the adenomatous polyposis coli (APC) tumor suppressor, a well conserved +TIP phosphoprotein with a pivotal function in cell cycle regulation. Another binding partner of the EB1-C domain is the well conserved +TIP protein dynactin, a component of the large cytoplasmic dynein/dynactin complex [1,2,3].

The ~80-residue EB1-C domain starts with a long smoothly curved helix (α1), which is followed by a hairpin connection leading to a short second helix (α2) running antiparallel to α1 (see <PDB:1WU9>). The two parallel α1 helices of the EB1-C domain dimer wrap around each other in a slightly left-handed supercoil. The two α2 helices run antiparallel to helices α1 and form a similar fork in the opposite orientation and rotated by 90. As a result, two helical segments from each monomer form a four-helix bundle. The side chain forming the hydrophobic core of this bundle are highly conserved [2,3,4].

Some protein known to contain a EB1-C domain are listed below:

  • Yeast protein BIM1.
  • Fission yeast microtubule integrity protein mal3.
  • Vertebrate microtubule-associated protein RP/EB family member 1 (EB1).
  • Vertebrate microtubule-associated protein RP/EB family member 2 (EB2 or RP1).
  • Vertebrate microtubule-associated protein RP/EB family member 3 (EBF3).

The profile we developed covers the entire EB1-C domain.

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Last update:

July 2006 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

EB1_C, PS51230; EB1-C terminal (EB1-C) domain profile  (MATRIX)


References

1AuthorsMathur J. Mathur N. Kernebeck B. Srinivas B.P. Huelskamp M.
TitleA novel localization pattern for an EB1-like protein links microtubule dynamics to endomembrane organization.
SourceCurr. Biol. 13:1991-1997(2003).
PubMed ID14614826

2AuthorsSlep K.C. Rogers S.L. Elliott S.L. Ohkura H. Kolodziej P.A. Vale R.D.
TitleStructural determinants for EB1-mediated recruitment of APC and spectraplakins to the microtubule plus end.
SourceJ. Cell Biol. 168:587-598(2005).
PubMed ID15699215
DOI10.1083/jcb.200410114

3AuthorsHonnappa S. John C.M. Kostrewa D. Winkler F.K. Steinmetz M.O.
TitleStructural insights into the EB1-APC interaction.
SourceEMBO J. 24:261-269(2005).
PubMed ID15616574
DOI10.1038/sj.emboj.7600529

4AuthorsHayashi I. Wilde A. Mal T.K. Ikura M.
TitleStructural basis for the activation of microtubule assembly by the EB1 and p150Glued complex.
SourceMol. Cell 19:449-460(2005).
PubMed ID16109370
DOI10.1016/j.molcel.2005.06.034



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

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