PMID:20691902

Citation	Subramanian, R, Wilson-Kubalek, EM, Arthur, CP, Bick, MJ, Campbell, EA, Darst, SA, Milligan, RA and Kapoor, TM (2010) Insights into antiparallel microtubule crosslinking by PRC1, a conserved nonmotor microtubule binding protein. Cell 142:433-43
Abstract	Formation of microtubule architectures, required for cell shape maintenance in yeast, directional cell expansion in plants and cytokinesis in eukaryotes, depends on antiparallel microtubule crosslinking by the conserved MAP65 protein family. Here, we combine structural and single molecule fluorescence methods to examine how PRC1, the human MAP65, crosslinks antiparallel microtubules. We find that PRC1's microtubule binding is mediated by a structured domain with a spectrin-fold and an unstructured Lys/Arg-rich domain. These two domains, at each end of a homodimer, are connected by a linkage that is flexible on single microtubules, but forms well-defined crossbridges between antiparallel filaments. Further, we show that PRC1 crosslinks are compliant and do not substantially resist filament sliding by motor proteins in vitro. Together, our data show how MAP65s, by combining structural flexibility and rigidity, tune microtubule associations to establish crosslinks that selectively "mark" antiparallel overlap in dynamic cytoskeletal networks.
Links	PubMed PMC2966277 Online version:10.1016/j.cell.2010.07.012
Keywords	Cell Cycle Proteins/chemistry; Cell Cycle Proteins/metabolism; Cryoelectron Microscopy; Humans; Microtubules/metabolism; Models, Molecular; Protein Structure, Tertiary; Spectrin/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
HUMAN:PRC1	enables	GO:0042802: identical protein binding	ECO:0000353: physical interaction evidence used in manual assertion	UniProtKB:O43663-1	F		Seeded From UniProt	complete

References

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