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Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
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There are three types of cytoskeletal structures in eukaryotic cells—microfilaments, intermediate filaments, and microtubules. With a diameter of about 25 nm, microtubules are the thickest of these fibers. Microtubules carry out a variety of functions that include cell structure and support, transport of organelles, cell motility (movement), and the separation of chromosomes during cell division.
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Microtubules are the thickest cytoskeletal filaments with a diameter of 25 nm. In prokaryotic organisms, microtubules are commonly found in locomotory appendages like cilia and flagella. In eukaryotic cells, microtubules form specialized extensions for moving fluid over the surface, like those found in cells lining the intestine.
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Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated...
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Microtubules are dynamic structures that undergo continuous assembly and disassembly. They originate from specialized multi-protein complexes known as microtubule organizing centers or MTOCs. Within the MTOC, the point of origin of the microtubule is known as the minus end, while the end radiating outward is the plus end. Microtubules serve two primary functions — the organization of spindle complexes to separate sister chromatids during mitotic or meiotic cell division and the formation...
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Mapping multivalency in the CLIP-170-EB1 microtubule plus-end complex.

Yaodong Chen1,2, Ping Wang3, Kevin C Slep4

  • 1From the Key Laboratory of Resources Biology and Biotechnology in Western China, Ministry of Education, College of Life Sciences, Northwest University, Xi'an, Shaanxi 710069, China.

The Journal of Biological Chemistry
|November 21, 2018
PubMed
Summary

Cytoplasmic linker protein 170 (CLIP-170) has multiple EB1-binding sites beyond its CAP-Gly domains. These novel serine-rich motifs enhance CLIP-170

Keywords:
CAP-GlyCLIP-170EB1SXIPcytoskeletonisothermal titration calorimetry (ITC)microtubulemicrotubule-associated protein (MAP)protein–protein interactiontubulin

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • Cytoplasmic linker protein 170 (CLIP-170) is crucial for linking vesicles to microtubules and recruiting dynein-dynactin complexes.
  • CLIP-170's localization to microtubule plus ends is dependent on end-binding 1 (EB1).
  • CLIP-170 features N-terminal cytoskeleton-associated protein glycine-rich (CAP-Gly) domains and serine-rich regions, with CAP-Gly domains known to bind EB1.

Purpose of the Study:

  • To identify and characterize novel EB1-binding determinants within the serine-rich regions of CLIP-170.
  • To elucidate the binding mechanisms and avidity of CLIP-170's interaction with EB1.
  • To understand how multiple EB1-binding modules contribute to CLIP-170's microtubule plus-end localization.

Main Methods:

  • Isothermal titration calorimetry (ITC) to measure binding thermodynamics.
  • Size-exclusion chromatography to assess protein complex formation and stoichiometry.
  • Biophysical characterization of CLIP-170 N-terminal EB1-binding modules.

Main Results:

  • Multiple EB1-binding modules were identified in CLIP-170's N-terminal region, including CAP-Gly domains, an SXIP motif, and novel SXIP-like motifs.
  • CLIP-170 CAP-Gly domains bind the EB1 EEY motif, allowing flanking SXIP and SXIP-like motifs to engage the EB homology domain.
  • These multivalent interactions provide avidity, explaining CLIP-170's preference for EB1 over α-tubulin and contributing to its localization.

Conclusions:

  • CLIP-170 possesses multiple non-CAP-Gly EB1-binding modules, expanding the known repertoire of EB1 interaction motifs.
  • The multivalent binding network enhances CLIP-170-EB1 avidity, influencing protein localization.
  • These findings offer insights into the regulation of microtubule plus-end dynamics and CLIP-170 function.