Ca2+-Dependent Inhibition of Actin-Activated Myosin ATPase Activity by S100C (S100A11), a Novel Member of the S100 Protein Family

Zhao, Xu; Naka, Michiko; Muneyuki, Mannosuke; Tanaka, Toshio

doi:10.1006/bbrc.1999.1918

Cited by 41 publications

(32 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Rad54B is a homolog of the DNA repair and recombination protein RAD54 as well as a DNA-dependent ATPase and seems to play an unique role in homologous recombination Tanaka et al, 2002). Additionally and as an internal control for the detection of protein-protein interactions in vivo using our approach, we confirmed the well-known protein interaction between S100A11 and actin ( Supplemental Figure S1; Xhao et al, 2000). The protein complex between S100A11 and actin occurs temporally and spatially in a manner different from the complex containing S100A11 and Rad54B, because S100A11 interacts with actin exclusively in the cytoplasm.…”

Section: Identification Of Rad54b As An Interactingsupporting

confidence: 72%

Rad54B Targeting to DNA Double-Strand Break Repair Sites Requires Complex Formation with S100A11

Murzik

Hemmerich

Weidtkamp‐Peters

et al. 2008

MBoC

View full text Add to dashboard Cite

S100A11 is involved in a variety of intracellular activities such as growth regulation and differentiation. To gain more insight into the physiological role of endogenously expressed S100A11, we used a proteomic approach to detect and identify interacting proteins in vivo. Hereby, we were able to detect a specific interaction between S100A11 and Rad54B, which could be confirmed under in vivo conditions. Rad54B, a DNA-dependent ATPase, is described to be involved in recombinational repair of DNA damage, including DNA double-strand breaks (DSBs). Treatment with bleomycin, which induces DSBs, revealed an increase in the degree of colocalization between S100A11 and Rad54B. Furthermore, S100A11/ Rad54B foci are spatially associated with sites of DNA DSB repair. Furthermore, while the expression of p21 WAF1/CIP1 was increased in parallel with DNA damage, its protein level was drastically down-regulated in damaged cells after S100A11 knockdown. Down-regulation of S100A11 by RNA interference also abolished Rad54B targeting to DSBs. Additionally, S100A11 down-regulated HaCaT cells showed a restricted proliferation capacity and an increase of the apoptotic cell fraction. These observations suggest that S100A11 targets Rad54B to sites of DNA DSB repair sites and identify a novel function for S100A11 in p21-based regulation of cell cycle. INTRODUCTIONProteins may exist in several complexes in a spatial and temporal manner to accomplish distinct functions. Analyses of the interacting partners will provide a strong insight into the physiological role of a particular factor. Therefore, it is essential to identify ideally all interacting partners of proteins in vivo to precisely be able to define their biological function. The investigation of protein complexes of solely endogenously expressed proteins avoid the tendency to detect false positive protein-protein interactions of examinations performed in vitro. A multitude of proteins are involved in both the detection and the repair of DNA damages. It is conceivable that some protein complexes involved in these processes are not yet discovered. A severe form of DNA damage that threaten the integrity of the genome are DNA double-strand breaks (DSBs). DSBs can lead to cell cycle arrest or illegitimate DNA rearrangements that can contribute to cell dysfunction, cell death, or carcinogenesis (Hoeijmakers, 2001). Homologous recombination is a major DNA repair pathway by which DSBs are repaired (Lettier et al., 2006).For the identification of specific interacting proteins of S100A11 (S100C, calgizzarin) we used in the present study a proteomic approach comprising mass spectrometry and immunological techniques. S100A11 belongs to the group of S100 proteins that are considered as multitasking proteins involved in several biological processes such as the Ca 2ϩ signaling network, cell growth and motility, cell cycle progression, transcription, and cell differentiation (Schafer and Heizmann, 1996;Donato, 2001;Eckert et al., 2004). It has been proposed that the S100 proteins are involved in...

show abstract

Section: Identification Of Rad54b As An Interactingsupporting

confidence: 72%

Rad54B Targeting to DNA Double-Strand Break Repair Sites Requires Complex Formation with S100A11

Murzik

Hemmerich

Weidtkamp‐Peters

et al. 2008

MBoC

View full text Add to dashboard Cite

show abstract

“…Because calcyclin was found to be associated with the nuclear envelope in a calcium-dependent manner (35), it was interesting to see if calcyclin might regulate phosphorylation of CacyBP by direct interaction with this protein. It has been reported that S100B inhibits phosphorylation of p53 by direct interaction and not by influencing the kinase activity (36) and that S100C inhibits actin-activated myosin ATPase in the same way (37 phenomenon might be stimulated or regulated by a phosphorylation process.…”

Section: Discussionmentioning

confidence: 95%

Ca2+-dependent Translocation of the Calcyclin-binding Protein in Neurons and Neuroblastoma NB-2a Cells

Filipek¹,

Jastrzębska²,

Nowotny³

et al. 2002

Journal of Biological Chemistry

View full text Add to dashboard Cite

“…Several other pseudopod-enriched proteins have also been reported to be associated with cancer including COTL1, YWHAE, ATP synthase, TPM4, SET, PTMA, and CNN2 (33)(34)(35)(36)(37)(38). Importantly, many of the identified proteins (Table 1), such as COTL1, YWHAE, TPM4, CNN2, septin 9, AHNAK, S100A11, and eIF4E, have well-defined associations with the actin cytoskeleton (39)(40)(41)(42)(43)(44)(45). In addition, we also identified five ribosomal proteins (RPL11, RPL23, RPL6A, RPL13, and RPL27) that, together with pseudopodial enrichment of eIF4E, elongation factor α (46), and various other proteins associated with RNA translocation and protein translation (19), further supports actin-rich pseudopodia as sites of active protein translation.…”

Section: Discussionmentioning

confidence: 98%

Pseudopodial Actin Dynamics Control Epithelial-Mesenchymal Transition in Metastatic Cancer Cells

et al. 2010

View full text Add to dashboard Cite

A key cellular process associated with the invasive or metastatic program in many cancers is the transformation of epithelial cells toward a mesenchymal state, a process called epithelial to mesenchymal transition or EMT. Actin-dependent protrusion of cell pseudopodia is a critical element of mesenchymal cell migration and therefore of cancer metastasis. However, whether EMT occurs in human cancers and, in particular, whether it is a prerequisite for tumor cell invasion and metastasis, remains a subject of debate. Microarray and proteomic analysis of actin-rich pseudopodia from six metastatic human tumor cell lines identified 384 mRNAs and 64 proteins common to the pseudopodia of six metastatic human tumor cell lines of various cancer origins leading to the characterization of 19 common pseudopod-specific proteins. Four of these (AHNAK, septin-9, eIF4E, and S100A11) are shown to be essential for pseudopod protrusion and tumor cell migration and invasion. Knockdown of each of these proteins in metastatic cells resulted in reduced actin cytoskeleton dynamics and induction of mesenchymal-epithelial transition (MET) that could be prevented by the stabilization of the actin cytoskeleton. Actin-dependent pseudopodial protrusion and tumor cell migration are therefore determinants of EMT. Protein regulators of pseudopodial actin dynamics may represent unique molecular targets to induce MET and thereby inhibit the metastatic potential of tumor cells.Cancer Res; 70(9); 3780-90. ©2010 AACR.

show abstract

Ca2+-Dependent Inhibition of Actin-Activated Myosin ATPase Activity by S100C (S100A11), a Novel Member of the S100 Protein Family

Cited by 41 publications

References 13 publications

Rad54B Targeting to DNA Double-Strand Break Repair Sites Requires Complex Formation with S100A11

Rad54B Targeting to DNA Double-Strand Break Repair Sites Requires Complex Formation with S100A11

Ca2+-dependent Translocation of the Calcyclin-binding Protein in Neurons and Neuroblastoma NB-2a Cells

Pseudopodial Actin Dynamics Control Epithelial-Mesenchymal Transition in Metastatic Cancer Cells

Contact Info

Product

Resources

About