Anionic regions in nuclear proteins.

Earnshaw, William C.

doi:10.1083/jcb.105.4.1479

Cited by 162 publications

(104 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…20), there is strong evidence to suggest a nuclear role: its C terminus region bears a karyophilic signal (21) and ProT␣ migrates to the nucleus in proliferating cells (22,23). Recent work in our laboratory has shown that ProT␣ binds histones and cooperates in nucleosome assembly in vitro (24), suggesting that the putative nuclear function may be related to chromatin remodeling; this possibility is consistent with the structural similarities between ProT␣ and various nuclear proteins known to be involved in chromatin activity (25,26).…”

supporting

confidence: 66%

A 180-kDa Protein Kinase Seems to Be Responsible for the Phosphorylation of Prothymosin α Observed in Proliferating Cells

Pérez-Estévez

Díaz-Jullien

Covelo

et al. 1997

Journal of Biological Chemistry

View full text Add to dashboard Cite

Prothymosin ␣ (ProT␣) is an acidic protein involved in cell proliferation. Its phosphorylation status is correlated with proliferative activity. Here we report the isolation and characterization of a ProT␣-phosphorylating kinase (ProT␣K) from mouse splenocytes that seems to be responsible for the in vivo phosphorylation of ProT␣ and that differs from other protein kinases reported to date. This enzyme, mainly located in the cytosol, has an molecular mass of 180 kDa and appears to be made up of two proteins of 64 and 60 kDa. Its activity was markedly enhanced by mitogenic activation of cells. The ProT␣ residues phosphorylated by the enzyme in vitro are a Thr at position 7 and another Thr at positions 12 or 13, both located within casein kinase 2 (CK-2) consensus motifs; these are the same residues as are phosphorylated in vivo. The new enzyme shows a number of clear structural and catalytic differences from CK-2. It phosphorylates histones H2B and H3, although with weaker activity than ProT␣. An enzyme with the same characteristics was also found in other murine tissues and cell lines.

show abstract

supporting

confidence: 66%

A 180-kDa Protein Kinase Seems to Be Responsible for the Phosphorylation of Prothymosin α Observed in Proliferating Cells

Pérez-Estévez

Díaz-Jullien

Covelo

et al. 1997

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Both SPT5 and SPT6 encode essential nuclear proteins with extremely acidic N termini and have been suggested to influence gene expression through a function in chromatin assembly or modification. Indeed, other proteins thought to interact with chromatin have similarly acidic regions (10). Furthermore, the gene dosage effects for SPT5 and SPT6 are similar to those for histone genes (5 (37) have demonstrated that the TATA-proximal heat shock element is required for basal expression of the HSP82 gene, implying that heat shock transcription factor is involved in basal-level expression of HSP82 as well as induction by heat shock.…”

Section: Discussionmentioning

confidence: 80%

CDC68, a yeast gene that affects regulation of cell proliferation and transcription, encodes a protein with a highly acidic carboxyl terminus.

Rowley¹,

Singer²,

Johnston³

1991

Mol. Cell. Biol.

122

120

View full text Add to dashboard Cite

The cell cycle of the budding yeast Saccharomyces cerevisiae has been investigated through the study of conditional cdc mutations that specificaUly affect cell cycle performance. Cells bearing the cdc68-1 mutation (J. A. Prendergast, L. E. Murray, A. Rowley, D. R. Carruthers, R. A. Singer, and G. C. Johnston, Genetics 124:81-90, 1990) are temperature sensitive for the performance of the G1 regulatory event, START. Here we describe the CDC68 gene and present evidence that the CDC68 gene product functions in transcription. CDC68 encodes a 1,035-amino-acid protein with a highly acidic and serine-rich carboxyl terminus. The abundance of transcripts from several unrelated genes is decreased in cdc68-1 mutant cells after transfer to the restrictive temperature, while at least one transcript, from the HSP82 gene, persists in an aberrant fashion. Thus, the cdc68-1 mutation has both positive and negative effects on gene expression. Our findings complement those of Malone et al.

show abstract

“…CaMK IV contains a polyglutamate-rich C-terminal tail (28), which is characteristic of chromatin-associated proteins (41). In the brain, CaMK IV is activated by CaM kinase kinase (CaMKK) (42,43) and inactivated by autophosphorylation within the CaM binding domain (44).…”

mentioning

confidence: 99%

Calcium/Calmodulin-dependent Protein Kinase IV Is Cleaved by Caspase-3 and Calpain in SH-SY5Y Human Neuroblastoma Cells Undergoing Apoptosis

McGinnis¹,

Whitton²,

Gnegy³

et al. 1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

We have previously demonstrated cleavage of ␣-spectrin by caspase-3 and calpain during apoptosis in SH-SY5Y neuroblastoma cells (Nath, R., Raser, K. J., Stafford, D., Hajimohammadreza, I., Posner, A., Allen, H., Talanian, R. V., Yuen, P., Gilbertsen, R. B., and Wang, K. K. (1996) Biochem. J. 319, 683-690). We demonstrate here that calcium/calmodulin-dependent protein kinase IV (CaMK IV) is cleaved during apoptosis by caspase-3 and calpain. We challenged SH-SY5Y cells with the proapoptotic agent thapsigargin. Western blot analysis revealed major CaMK IV breakdown products of 40, 38, and 33 kDa. Digestion of control SH-SY5Y lysate with purified caspase-3 produced a 38-kDa CaMK IV fragment; digestion with purified calpain produced a major fragment of 40 kDa. Pretreatment with carbobenzoxyAsp-CH 2 OC(O)-2,6-dichlorobenzene or Z-Val-Ala-Aspfluoromethylketone was able to block the caspase-3-mediated production of the 38-kDa fragment both in situ and in vitro. Calpain inhibitor II similarly blocked formation of the calpain-mediated 40-kDa fragment both in situ and in vitro. Digestion of recombinant CaMK IV by other caspase family members revealed that only caspase-3 produces a fragmentation pattern consistent to that seen in situ. The major caspase-3 and calpain cleavage sites are respectively identified as PAPD 176 *A and CG 201 *A, both within the CaMK IV catalytic domain. Furthermore, calmodulin-stimulated protein kinase activity decreases within 6 h in thapsigargin-treated SH-SY5Y. The loss of activity precedes cell death.

show abstract

Anionic regions in nuclear proteins.

Cited by 162 publications

References 48 publications

A 180-kDa Protein Kinase Seems to Be Responsible for the Phosphorylation of Prothymosin α Observed in Proliferating Cells

A 180-kDa Protein Kinase Seems to Be Responsible for the Phosphorylation of Prothymosin α Observed in Proliferating Cells

CDC68, a yeast gene that affects regulation of cell proliferation and transcription, encodes a protein with a highly acidic carboxyl terminus.

Calcium/Calmodulin-dependent Protein Kinase IV Is Cleaved by Caspase-3 and Calpain in SH-SY5Y Human Neuroblastoma Cells Undergoing Apoptosis

Contact Info

Product

Resources

About