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2 Seema TRIVEDI the nucleation site from kinetochores (reviewed in Raff, 2002). The complex associates at the plus ends of the MTs growing out from the centrosome during nucleation (reviewed in Raff, 2002). However, the exact mechanism by which TACC interacts with other MAPs and recruits them to the centrosome is not clearly understood. In Drosophila, D-TACC recruits Mini spindles protein (Msps; a conserved family of MAP) (reviewed in Raff, 2002) and in Xenopus, maskin (TACC3) form a complex with XMAP215 (Albee and Wiese, 2008). However, the XMAP215 complex may associate with both plus and minus ends of the MT. Similarly, human TACCs and ch-TOG (colonic– hepatic tumour-overexpressed gene) (homologue of Msps) possibly form a structural lattice at centrosomes to maintain the integrity of spindle poles and to stabilize spindle MTs (reviewed in Raff, 2002; Gergely et al., 2003). However, it is not known why in cultured human cells TACC3 and, in Drosophila D-TACC, these proteins are apparently not essential for recruitment of XMAP215 analogue (Brittle and Ohkura, 2005). This review focuses on genomic locations, protein characteristics and interactions of TACC proteins in humans and general aspects of role of TACC proteins in spindle dynamics in higher eukaryotes. TACC genes and proteins Three TACC proteins have been identified in humans, namely TACC1, 2 and 3. The three human TACCs are related by ~200-amino-acid C-terminal region (the ‘TACC domain’), which is predicted to form a coiled coil domain (reviewed in Raff, 2002). Besides TACC domain, these proteins share homology (except Drosophila D-TACC) in the SDP domain as well (Lauffart et al., 2002; Still et al., 2004). SDP domain is composed of functionally conserved repeats of 33 amino acids, though the numbers of repeats are different in different TACC proteins. Interaction of SDP domain with transcription factor GAS41/NuBI1 (also known as YEATS4) has been established (Lauffart et al., 2002) but this interaction possibly does not directly affect spindle formation. Genomic locations of human TACC reference gene sequences as per NCBI and details of proteins obtained from SwissProt are given in Table 1. Though implicated in several cancers, no mutations have been reported in the TACC1 gene (Still et al., 2008). TACC1 mRNA exon 3 contains a predicted nuclear localization signal (Still et al., 2008), shows ubiquitous expression and encodes a cytoplasmic protein which is mainly perinuclear protein (molecular mass of 125 kDa) (Conte et al., 2002) but different isoforms in different cells may be localized in the cytoplasm as well (Lauffart et al., 2006). TACC1 protein does not show compositional bias whereas TACC2 has poly-lysine and poly-proline rich regions and TACC3 has poly-serine regions (Table 1). In addition, different sites in the TACC proteins show post translational covalent modifications (Table 2). Phosphotyrosine is seen only in TACC1, while N6-acetyl lysine is seen only in TACC3 and phosphothreonine is not seen in TACC1. It is also pertinent to note that TACC1 phosphorylation varies in different isoforms (Still et al., 2008). TACC2 concentration at the centrosome has been observed even during interphase unlike TACC1 and TACC3 proteins (Gergley et al., 2000a). TACC3, also known as ERIC1 (Still et al., 2004; Eslinger et al., 2009) a non-motor MAP, was also identified as an ARNT interacting protein (Aint1) in mice (Aitola et al., 2003) and is expressed in proliferative tissues (Aitola et al., 2003; reviewed in Hood and Royle, 2011). During mitosis, TACC3 is localized to centrosome but during interphase, TACC3 is seen in cytoplasmic or perinuclear regions (Piekorz et al., 2002). The TACC3 gene has five reported mutations: CAG to CGG, TCG to TTG, CGT to TGT, CAG to TAG and TCA to TTA (Eslinger et al., 2009).
TACC proteins in spindles 3 Table 1. Human TACC Genomic Location (as per NCBI + ), Introns, mRNA And Splice Variants (as per NCBI AceView + ) and Protein Details (as per SwissProt * ). Official Symbol TACC1 TACC2 TACC3 Genomic Location 8p11.22 10q26 4p16.3 Genomic Sequence NC_000008.10 38585704..38710546 NC_000010.10 123748689..124014057 NC_000004.11 1723266..1746898 Number of Introns + 44 49 23 mRNA + 38 (7 unspliced) 35 (7 unspliced) 16 (3 unspliced) Protein * TACC1 (O75410 TACC1_HUMAN) TACC2 (O95359 TACC2_HUMAN) TACC3 (Q9Y6A5 TACC3_HUMAN) Length (number of amino acids) 805 2948 838 Number of Isoforms + 27 26 15 Features Description Coiled coil Potential Compositional bias Domain Motif Region TACC1 610 - 805 Position TACC2 TACC3 2675 - 2703 637 - 837 2746 - 2947 Poly-Lys 2420 - 2423 Poly-Ser 155 - 160 Pro-rich 1956 - 2016 482 - 549 SPAZ 2315 - 2403 SPAZ 1 215 - 297 SPAZ 2 359 - 507 Bipartite nuclear localization 226 - 241 signal 1 Potential Bipartite nuclear localization 455 - 471 signal 2 Potential Interaction with CH-TOG Interaction with LSM7 and SNRPG Interaction with TDRD7 Interaction with YEATS4 701 - 805 1 - 55 152 - 259 206 - 427 + Thierry-Mieg and Thierry-Mieg 2006, AceView-Dec 2009
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