4L6Y
Structure of the microtubule associated protein PRC1 (Protein Regulator of Cytokinesis 1)
Summary for 4L6Y
Entry DOI | 10.2210/pdb4l6y/pdb |
Related | 4L3I |
Descriptor | Protein regulator of cytokinesis 1 (1 entity in total) |
Functional Keywords | spectrin, microtubule binding; microtubule crosslinking, microtubule; kinesin-4, spindle midzone, structural protein |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus : O43663 |
Total number of polymer chains | 2 |
Total formula weight | 116365.32 |
Authors | Subramanian, R.,Ti, S.,Tan, L.,Darst, S.A.,Kapoor, T.M. (deposition date: 2013-06-13, release date: 2013-07-17, Last modification date: 2023-09-20) |
Primary citation | Subramanian, R.,Ti, S.C.,Tan, L.,Darst, S.A.,Kapoor, T.M. Marking and Measuring Single Microtubules by PRC1 and Kinesin-4. Cell(Cambridge,Mass.), 154:377-390, 2013 Cited by PubMed Abstract: Error-free cell division depends on the assembly of the spindle midzone, a specialized array of overlapping microtubules that emerges between segregating chromosomes during anaphase. The molecular mechanisms by which a subset of dynamic microtubules from the metaphase spindle are selected and organized into a stable midzone array are poorly understood. Here, we show using in vitro reconstitution assays that PRC1 and kinesin-4, two microtubule-associated proteins required for midzone assembly, can tag microtubule plus ends. Remarkably, the size of these tags is proportional to filament length. We determine the crystal structure of the PRC1 homodimer and map the protein-protein interactions needed for tagging microtubule ends. Importantly, length-dependent microtubule plus-end-tagging by PRC1 is also observed in dividing cells. Our findings suggest how biochemically similar microtubules can be differentially marked, based on length, for selective regulation during the formation of specialized arrays, such as those required for cytokinesis. PubMed: 23870126DOI: 10.1016/j.cell.2013.06.021 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.3015 Å) |
Structure validation
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