DYNLT3 is a member of the dynein motor protein family. DYNLT3 binds to BUB3, a spindle checkpoint protein is present on kinetochores at prometaphase.[3] DYNLT3 can also function as a transcription regulator of Bcl-2 gene through binding to SATB1 in a dynein-independent manner.[4]
↑Roux AF, Rommens J, McDowell C, Anson-Cartwright L, Bell S, Schappert K, Fishman GA, Musarella M (February 1994). "Identification of a gene from Xp21 with similarity to the tctex-1 gene of the murine t complex". Hum. Mol. Genet. 3 (2): 257–63. doi:10.1093/hmg/3.2.257. PMID8004092.
↑Lo KW, Kogoy JM, Pfister KK (April 2007). "The DYNLT3 light chain directly links cytoplasmic dynein to a spindle checkpoint protein, Bub3". J. Biol. Chem. 282 (15): 11205–12. doi:10.1074/jbc.M611279200. PMID17289665.
↑Yeh TY, Chuang JZ, Sung CH (August 2005). "Dynein light chain rp3 acts as a nuclear matrix-associated transcriptional modulator in a dynein-independent pathway". J. Cell Sci. 118 (Pt 15): 3431–43. doi:10.1242/jcs.02472. PMID16079286.
↑Schwarzer, Christian; Barnikol-Watanabe Shitsu; Thinnes Friedrich P; Hilschmann Norbert (Sep 2002). "Voltage-dependent anion-selective channel (VDAC) interacts with the dynein light chain Tctex1 and the heat-shock protein PBP74". Int. J. Biochem. Cell Biol. 34 (9): 1059–70. doi:10.1016/S1357-2725(02)00026-2. ISSN1357-2725. PMID12009301.
Further reading
Roux AF, Rommens J, McDowell C, et al. (1994). "Identification of a gene from Xp21 with similarity to the tctex-1 gene of the murine t complex". Hum. Mol. Genet. 3 (2): 257–63. doi:10.1093/hmg/3.2.257. PMID8004092.
Mueller S, Cao X, Welker R, Wimmer E (2002). "Interaction of the poliovirus receptor CD155 with the dynein light chain Tctex-1 and its implication for poliovirus pathogenesis". J. Biol. Chem. 277 (10): 7897–904. doi:10.1074/jbc.M111937200. PMID11751937.
Schwarzer C, Barnikol-Watanabe S, Thinnes FP, Hilschmann N (2002). "Voltage-dependent anion-selective channel (VDAC) interacts with the dynein light chain Tctex1 and the heat-shock protein PBP74". Int. J. Biochem. Cell Biol. 34 (9): 1059–70. doi:10.1016/S1357-2725(02)00026-2. PMID12009301.
Douglas MW, Diefenbach RJ, Homa FL, et al. (2004). "Herpes simplex virus type 1 capsid protein VP26 interacts with dynein light chains RP3 and Tctex1 and plays a role in retrograde cellular transport". J. Biol. Chem. 279 (27): 28522–30. doi:10.1074/jbc.M311671200. PMID15117959.