Chinese hamster protein homologous to human putative protein kinase KIAA0204 is associated with nuclei, microtubules and centrosomes in CHO‐K1 cells

Zinovkina, L. A.; Полтараус, А. Б.; Solovyanova, Olga B; Nadezhdina, E. S.

doi:10.1016/s0014-5793(97)00952-6

Cited by 12 publications

(19 citation statements)

References 29 publications

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“…In our previous work we have shown that the protein kinase LOSK was associated with microtubules and centrosome in CHO-K1 cell culture and in fish sperm (Zinovkina et al, 1997(Zinovkina et al, , 1998Nadezhdina et al, 2001). We proved it with immunofluorescence staining, immunoelectron microscopy, and cosedimentation with microtubules.…”

Section: Full-length Losk Partially Colocalizes With Microtubules Whmentioning

confidence: 60%

“…LOSK distributed mostly in cytoplasm is not a specific centrosomal protein. However, it was found in isolated sperm basal bodies and in centrosomes in cell culture (Zinovkina et al, 1997;Nadezhdina et al, 2001). Among potential centrosomal targets of LOSK (probably indirect) the tempting one is dynactin that localizes both in centrosomes and in the cytoplasm.…”

Section: Discussionmentioning

confidence: 99%

“…The rabbit polyclonal affinity-purified pol3D2 antibody against the LOSK structural domain was described previously (Zinovkina et al, 1997(Zinovkina et al, , 1998. To develop an anti-LOSK N-terminal domain antibody polKIA, LOSK-⌬T-pQE30 was expressed in Escherichia coli; 6His-LOSK-⌬T protein was purified in Ni-NTA column (Qiagen) and used for rabbit immunization and serum affinity fractionation.…”

Section: Antibodiesmentioning

confidence: 99%

“…More protein kinases are expected to be involved in the organization of microtubule arrays. LOSK (Long Ste20-like Kinase), a member of the germinal center kinase group, was identified as a microtubule and centrosome-associated protein (Zinovkina et al, 1997(Zinovkina et al, , 1998Nadezhdina et al, 2001). We expected that it participates in the regulation of centrosomal function or microtubule organization.…”

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confidence: 98%

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Ste20-related Protein Kinase LOSK (SLK) Controls Microtubule Radial Array in Interphase

Burakov

Zhapparova

Kovalenko

et al. 2008

MBoC

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Interphase microtubules are organized into a radial array with centrosome in the center. This organization is a subject of cellular regulation that can be driven by protein phosphorylation. Only few protein kinases that regulate microtubule array in interphase cells have been described. Ste20-like protein kinase LOSK (SLK) was identified as a microtubule and centrosome-associated protein. In this study we have shown that the inhibition of LOSK activity by dominant-negative mutant K63R-⌬T or by LOSK depletion with RNAi leads to unfocused microtubule arrangement. Microtubule disorganization is prominent in Vero, CV-1, and CHO-K1 cells but less distinct in HeLa cells. The effect is a result neither of microtubule stabilization nor of centrosome disruption. In cells with suppressed LOSK activity centrosomes are unable to anchor or to cap microtubules, though they keep nucleating microtubules. These centrosomes are depleted of dynactin. Vero cells overexpressing K63R-⌬T have normal dynactin "comets" at microtubule ends and unaltered morphology of Golgi complex but are unable to polarize it at the wound edge. We conclude that protein kinase LOSK is required for radial microtubule organization and for the proper localization of Golgi complex in various cell types. INTRODUCTIONThe radial array of microtubules is typical for many mammalian cells. It organizes bidirectional organelle transport in the cytoplasm in the endocytotic and exocytotic direction. It is also required for the regulation of interaction of microtubule plus ends with cell periphery. Both functions are important for cell polarization, movement, and signal transduction (Hyman and Karsenti, 1996;Dujardin et al., 2003;Morrison, 2007). The degree of radiality of microtubules varies in different types of cells. For instance, in fish melanophores the system of microtubules is perfectly radial (Schliwa et al., 1978), whereas in myotubes it is unclear (Tassin et al., 1985;Musa et al., 2003). Moreover, among fibroblast-like cultured mammalian cells some (green monkey kidney Vero or Chinese hamster ovary CHO-K1) possess a distinct radial microtubule array (Bre et al., 1987), whereas others (human cervical carcinoma HeLa or mouse fibroblasts NIH 3T3) have rather chaotic microtubule arrangements (Bulinski and Borisy, 1980). Regardless of the tissue origin of cells, microtubules become more radial when cultured cells are sparse and less radial in confluent cultures. It seems that the status of microtubule organization is regulated by signal transduction pathways and depends on cell differentiation.The focused microtubule arrays can also be formed in acentrosomal cell fragments as a result of interactions between microtubules and membrane vesicles, covered with motor proteins (Rodionov and Borisy, 1997;Malikov et al., 2005). In acentrosomal fragments of fish melanocytes microtubules are chaotic when pigment granules are dispersed. After the addition of adrenaline or other activation of melanosome aggregation microtubules assemble in a radial array. Thus, in this case...

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Section: Full-length Losk Partially Colocalizes With Microtubules Whmentioning

confidence: 60%

Section: Discussionmentioning

confidence: 99%

Section: Antibodiesmentioning

confidence: 99%

mentioning

confidence: 98%

See 2 more Smart Citations

Ste20-related Protein Kinase LOSK (SLK) Controls Microtubule Radial Array in Interphase

Burakov

Zhapparova

Kovalenko

et al. 2008

MBoC

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“…In the kidney SLK is found in tubular and glomerular epithelial cells (GECs; podocytes) 2 (10). Subcellularly, SLK is localized in the cytosol, nucleus, microtubules, and centrosomes (11,12). The regulation and functions of SLK have received considerable attention in recent years.…”

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confidence: 99%

Regulation of the Ste20-like Kinase, SLK

Luhovy

Jaberi

Papillon

et al. 2012

Journal of Biological Chemistry

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Background: SLK promotes apoptosis and may control cell survival during renal injury or repair. Results: Mutations in serine and threonine residues in the activation segment of SLK reduced kinase activity. Conclusion: Phosphorylation of SLK plays a key role in activation and signaling. Significance: Understanding the regulation of SLK activity is essential for developing novel therapeutic approaches to renal injury.

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SLK/LOSK kinase regulates cell motility independently of microtubule organization and Golgi polarization

et al. 2016

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Cell motility is an essential complex process that requires actin and microtubule cytoskeleton reorganization and polarization. Such extensive rearrangement is closely related to cell polarization as a whole. The serine/threonine kinase SLK/LOSK is a potential regulator of cell motility, as it phosphorylates a series of cytoskeleton-bound proteins that collectively participate in the remodeling of migratory cell architecture. In this work, we report that SLK/LOSK is an indispensable regulator of cell locomotion that primarily acts through the small GTPase RhoA and the dynactin subunit p150(Glued). Both RhoA and dynactin affect cytoskeleton organization, polarization, and general cell locomotory activity to various extents. However, it seems that these events are independent of each other. Thus, SLK/LOSK kinase effectively functions as a switch that links all of the processes underlying cell motility to provide robust directional movement.

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Chinese hamster protein homologous to human putative protein kinase KIAA0204 is associated with nuclei, microtubules and centrosomes in CHO‐K1 cells

Cited by 12 publications

References 29 publications

Ste20-related Protein Kinase LOSK (SLK) Controls Microtubule Radial Array in Interphase

Ste20-related Protein Kinase LOSK (SLK) Controls Microtubule Radial Array in Interphase

Regulation of the Ste20-like Kinase, SLK

SLK/LOSK kinase regulates cell motility independently of microtubule organization and Golgi polarization

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