title: Posttranslational protein modifications in cilia and flagella.
abstract: Tubulin and other flagellar and ciliary proteins are the substrates for a host of posttranslational modifications (PTMs), many of which have been highly conserved over evolutionary time. In addition to the binding of MAPs (microtubule-associated proteins) that provide a specific functionality, or the use of different tubulin isotypes to convey a specific function, most cells rely on an array of PTMs. These include phosphorylation, acetylation, glycylation, glutamylation, and methylation. The first and the last of this list are not unique to the tubulin in cilia and flagella, while the others are. This chapter will review briefly these varying modifications and will conclude with detailed methods for their detection and localization at the limit of resolution provided by electron microscopy.
authors.affiliation: Biological Sciences, Dartmouth College, Hanover, New Hampshire 03755, USA.
authors.forename: Roger D
authors.initials: RD
authors.lastname: Sloboda
mesh_terms: D000818:Animals; D002923:Cilia / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D005407:Flagella / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D007150:Immunohistochemistry; D008854:Microscopy, Electron / Q000295:instrumentation / Q000379:methods; D008870:Microtubules / Q000378:metabolism / Q000648:ultrastructure; D011499:Protein Processing, Post-Translational; D014404:Tubulin / Q000737:chemistry / Q000378:metabolism
chemical_list: D014404:Tubulin