pp39mos is associated with p34cdc2 kinase in c-mosxe-transformed NIH 3T3 cells.

Zhou, Renping; Daar, Ira; Ferris, Douglas K.; Ga, White; Paules, Richard S.; Woude, GF Vande

doi:10.1128/mcb.12.8.3583

Cited by 18 publications

(16 citation statements)

References 31 publications

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“…In this study, we further demonstrate from the GST pull-down assay that CagSpin directly or indirectly associates with h-tubulin, and therefore provide the first biochemical evidence for the specific interaction of Spindlin protein and h-tubulin, the microtubule component. Interestingly, some important proteins that play crucial functions during oocyte maturation and egg fertilization, such as p39 mos (Zhou et al, 1992;Haccard et al, 1993;Verlhac et al, 1996), p34 cdc2 of metaphase promoting factor (MPF) (Langan et al, 1989;Peter et al, 1990;Verde et al, 1990;Zhou et al, 1991Zhou et al, , 1992, cyclin B, the regulatory component of MPF (Pines and Hunter, 1991;Ookata et al, 1993), MAP kinase (Verlhac et al, 1993) and PKC (Page Baluch et al, 2004), have been also confirmed to associate with microtubules. Interestingly, three putative PKC phosphorylation sites have been revealed in the CagSpin sequence (Fig.…”

Section: Biochemical Evidence Of Association Between B-tubulin and Camentioning

confidence: 99%

Identification of a Spindlin homolog in gibel carp (Carassius auratus gibelio)

Wang

Sun

Mei

et al. 2005

Comparative Biochemistry and Physiology Part B: Biochemistry an

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Section: Biochemical Evidence Of Association Between B-tubulin and Camentioning

confidence: 99%

Identification of a Spindlin homolog in gibel carp (Carassius auratus gibelio)

Wang

Sun

Mei

et al. 2005

Comparative Biochemistry and Physiology Part B: Biochemistry an

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“…The washed pellets were resolved by SDS-PAGE and transferred to nitrocellulose filters. The lanes corresponding to the unlabelled proteins were immunoblotted with either ␣-or ␤-tubulin antibody, while the lanes corresponding to the 35 Slabelled lysate were exposed directly to autoradiography. We observed that the two predominant bands precipitated when the GST-Myc II was incubated with 35 S-labelled extracts comigrated with ␣-and ␤-tubulins (Fig.…”

Section: Specific Binding Of C-myc To Tubulin In Vitromentioning

confidence: 99%

The N-Terminal Domain of c-Myc Associates with α-Tubulin and Microtubules In Vivo and In Vitro

Alexandrova

Nikliński

Bliskovsky

et al. 1995

Molecular and Cellular Biology

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The polymerization of ␣-and ␤-tubulin into microtubules results in a complex network of microfibrils that have important structural and functional roles in all eukaryotic cells. In addition, microtubules can interact with a diverse family of polypeptides which are believed to directly promote the assembly of microtubules and to modulate their functional activity. We have demonstrated that the c-Myc oncoprotein interacts in vivo and in vitro with ␣-tubulin and with polymerized microtubules and have defined the binding site to the N-terminal region within the transactivation domain of c-Myc. In addition, we have shown that c-Myc colocalizes with microtubules and remains tightly bound to the microtubule network after detergent extraction of intact cells. These findings suggest a potential role for Myc-tubulin interaction in vivo.The product of the c-myc gene is a nuclear phosphoprotein that has been implicated in the regulation of cell differentiation, apoptosis, and the development of human tumors (5,19,28). The c-Myc protein includes multifunctional domains that include an N-terminal transactivation domain within exon II and a C-terminal domain, within exon III, which is necessary for heterodimerization (5, 19). These observations have supported the model that c-Myc functions as a transcription factor whose activity can be regulated by its protein binding partners. In addition, the N-terminal transactivation region of c-Myc binds to the retinoblastoma protein-related tumor suppressor protein p107, and it has been recently shown that this interaction can suppress the activity of the c-Myc transactivation domain (12). Further, the observation that Burkitt's lymphoma frequently contains naturally occurring somatic mutations within the transactivation domain (3, 34) which result in loss of p107 suppression confirms that this is an important functional domain of c-Myc.Although c-Myc is characterized as a nuclear protein (10, 15), it has recently been proposed that the subcellular localization of c-Myc can vary according to the proliferation state of the cell. For example, in actively growing NIH 3T3 cells c-Myc is predominantly found in the nucleus, while a shift to the cytoplasm occurs in contact-inhibited cells (31). An increased cytoplasmic/nuclear ratio for c-Myc has also been noted following monocytic differentiation of human myeloid leukemia cells (8) and in nondividing prefertilized Xenopus oocytes (14). In addition, comparison of c-Myc localization patterns of normal tissue, adenomas, and colorectal tumors showed that tumor progression was associated with an accumulation of cytoplasmic c-Myc protein (27). These experiments suggested that nucleus-cytoplasm exchanges of c-Myc protein play an important functional role in cell proliferation. Since it had been proposed that tubulin mediates the cytoplasm-to-nucleus translocation of the glucocorticoid and vitamin D receptors (2, 25), we examined whether c-Myc could also interact with tubulin and microtubules. This hypothesis was also suggested by the observation tha...

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“…Although several cMos-interacting proteins have been described (Zhou et al, 1991a(Zhou et al, , 1992Bai et al, 1992aBai et al, ,b, 1993Cooper, 1995, 1997;Chen et al, 1997), which help to explain the basis of c-Mos function in oocyte maturation and cellular transformation, regulation of c-Mos activity is still poorly understood. In this study we provide evidence that Hsp70 molecular chaperone is a major Mos-associated protein.…”

Section: Introductionmentioning

confidence: 99%