Kif17 phosphorylation regulates its ciliary localization and photoreceptor outer segment turnover

Lewis, Tylor R.; Kundinger, Sean R.; Link, Brian A.; Insinna, Christine; Besharse, Joseph C.

doi:10.1101/351122

Cited by 1 publication

(1 citation statement)

References 47 publications

(95 reference statements)

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“…For homodimeric Kif17, CaMKII-dependent phosphorylation of S1029 at the tail domain in dendrites disrupted its interaction with the scaffold protein Mint-1, which associates with vesicles carrying the NMDA receptors subunit GluN2B (Guillaud et al, 2008;Yin et al, 2012). Whereas the phosphorylation of S815 residue of zebrafish Kif17, which is equivalent to the S1029 of mouse Kif17, increased disc shedding and the motor turnover in the cone photoreceptor outer segment (Lewis et al, 2018). The S815 phosphorylation was suggested to facilitate Kif17 entry into the cilia.…”

Section: Phosphoregulation Of Kinesin-2mentioning

confidence: 99%

Phosphoregulation of Kinesins Involved in Long-Range Intracellular Transport

Kumari

Ray

2022

Front. Cell Dev. Biol.

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Kinesins, the microtubule-dependent mechanochemical enzymes, power a variety of intracellular movements. Regulation of Kinesin activity and Kinesin-Cargo interactions determine the direction, timing and flux of various intracellular transports. This review examines how phosphorylation of Kinesin subunits and adaptors influence the traffic driven by Kinesin-1, -2, and -3 family motors. Each family of Kinesins are phosphorylated by a partially overlapping set of serine/threonine kinases, and each event produces a unique outcome. For example, phosphorylation of the motor domain inhibits motility, and that of the stalk and tail domains induces cargo loading and unloading effects according to the residue and context. Also, the association of accessory subunits with cargo and adaptor proteins with the motor, respectively, is disrupted by phosphorylation. In some instances, phosphorylation by the same kinase on different Kinesins elicited opposite outcomes. We discuss how this diverse range of effects could manage the logistics of Kinesin-dependent, long-range intracellular transport.

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Section: Phosphoregulation Of Kinesin-2mentioning

confidence: 99%