8WHM
Crystal structure of the ELKS2/LL5beta complex
Summary for 8WHM
| Entry DOI | 10.2210/pdb8whm/pdb |
| Related | 8WHH |
| Descriptor | ERC protein 2, Pleckstrin homology-like domain family B member 2 (3 entities in total) |
| Functional Keywords | complex, protein binding |
| Biological source | Rattus norvegicus (Norway rat) More |
| Total number of polymer chains | 2 |
| Total formula weight | 17412.64 |
| Authors | |
| Primary citation | Jia, X.,Lin, L.,Guo, S.,Zhou, L.,Jin, G.,Dong, J.,Xiao, J.,Xie, X.,Li, Y.,He, S.,Wei, Z.,Yu, C. CLASP-mediated competitive binding in protein condensates directs microtubule growth. Nat Commun, 15:6509-6509, 2024 Cited by PubMed Abstract: Microtubule organization in cells relies on targeting mechanisms. Cytoplasmic linker proteins (CLIPs) and CLIP-associated proteins (CLASPs) are key regulators of microtubule organization, yet the underlying mechanisms remain elusive. Here, we reveal that the C-terminal domain of CLASP2 interacts with a common motif found in several CLASP-binding proteins. This interaction drives the dynamic localization of CLASP2 to distinct cellular compartments, where CLASP2 accumulates in protein condensates at the cell cortex or the microtubule plus end. These condensates physically contact each other via CLASP2-mediated competitive binding, determining cortical microtubule targeting. The phosphorylation of CLASP2 modulates the dynamics of the condensate-condensate interaction and spatiotemporally navigates microtubule growth. Moreover, we identify additional CLASP-interacting proteins that are involved in condensate contacts in a CLASP2-dependent manner, uncovering a general mechanism governing microtubule targeting. Our findings not only unveil a tunable multiphase system regulating microtubule organization, but also offer general mechanistic insights into intricate protein-protein interactions at the mesoscale level. PubMed: 39095354DOI: 10.1038/s41467-024-50863-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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