Targeting of γ-tubulin complexes to microtubule organizing centers: conservation and divergence

• MT nucleation templates are assembled via self-oligomerization of γ-TuSCs promoted by receptors and/or GCP4–6-dependent pathways.
• Both pathways ensure that γ-TuC localization and template assembly are intertwined events.
• The complexity and diversity of γ-TuC recruiting factors have evolved with types of mitosis.

Organisms with closed or open mitosis have differentially evolved various gamma-tubulin complex (γ-TuC) recruiting factors to organize diverse cellular microtubule (MT) arrays, including the mitotic spindle. γ-TuC recruiting factors not only target the γ-TuC to MT nucleation sites, but also regulate MT nucleation activity by generating the template for MT nucleation or promoting the MT nucleation activity of pre-existing γ-tubulin ring complexes (γ-TuRCs). Here we outline the current understanding of MT nucleator assembly and its regulation by γ-tubulin small complex (γ-TuSC) receptors. Moreover, we discuss the emergence of γ-TuC recruiting factors through evolution with augmented complexity and diversity and propose a hypothesis to account for the evolution of these factors in cooperative spindle assembly.