Open AccessFAM29A, a target of Plk1 regulation, controls the partitioning of NEDD1 between the mitotic spindle and the centrosomes
Author(s) -
Hui Zhu,
Kayleen Fang,
Guowei Fang
Publication year - 2009
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.048223
Subject(s) - centrosome , plk1 , biology , microbiology and biotechnology , spindle apparatus , polo like kinase , spindle pole body , mitosis , microtubule , multipolar spindles , kinetochore , microtubule nucleation , cell division , cell cycle , genetics , cell , gene , chromosome
We previously showed that FAM29A, a spindle-associated protein, promotes microtubule-dependent microtubule amplification through its interaction with and recruitment of NEDD1, the targeting subunit of the gamma-tubulin ring complex. We report here that FAM29A is regulated by Plk1, a kinase essential for spindle assembly and its bipolarity. Plk1, FAM29A and NEDD1 form three separate complexes in vivo, not one single complex. Plk1 recruits FAM29A to spindle microtubules, which, in turn, targets NEDD1 to the spindle. Plk1 also recruits NEDD1 to the centrosomes, probably through a Plk1-NEDD1 interaction, but this interaction does not contribute to targeting NEDD1 to the spindle. Altering intracellular levels of FAM29A changes the distribution of NEDD1 between the centrosomes and the spindle, indicating that FAM29A controls the partition of NEDD1 between these two mitotic structures. Thus, Plk1 promotes microtubule nucleation from the centrosomes through a FAM29A-independent pathway and from the spindle through a FAM29A-dependent pathway. FAM29A controls the relative contributions of these two pathways to microtubule polymerization during mitosis.