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Gas2  -  growth arrest specific 2

Mus musculus

Synonyms: GAS-2, Gas-2, Growth arrest-specific protein 2
 
 
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High impact information on Gas2

  • Here we provide evidence that overexpression of Gas2 efficiently increases cell susceptibility to apoptosis following UV irradiation, etoposide and methyl methanesulfonate treatments, and that these effects are dependent on increased p53 stability and transcription activity [1].
  • Gas2 is a caspase-3 substrate that plays a role in regulating microfilament and cell shape changes during apoptosis [1].
  • At its COOH terminus, mACF7 contains two putative EF-hand calcium-binding motifs and a segment homologous to the growth arrest-specific protein, Gas2 [2].
  • After serum or growth factor addition to quiescent NIH 3T3 cells, Gas2 is hyperphosphorylated and relocalized at the membrane ruffles [3].
  • The evidence accumulated here could thus represent a first example of a mechanism linking apoptosis with the co-ordinated microfilament-dependent cell shape changes, as possibly mediated by an interleukin-1 beta-converting enzyme (ICE)-like dependent proteolytic cleavage of the Gas2 protein [3].
 

Biological context of Gas2

  • We demonstrate that during apoptosis the C-terminal domain of Gas2 is removed by proteolytic cleavage, resulting in a protein that is similar in size to the described delta 276-314 [3].
  • Gas2 seems to be regulated also at the posttranslational level via a phosphorylation mechanism [4].
  • Moreover, by using in vitro mutagenesis, we also demonstrate that the proteolytic processing of Gas2 during apoptosis is dependent on an aspartic acid residue at position 279 [3].
  • In vivo proteolysis of Gas2 was detected at an early stage of the apoptotic process when the cells are still adherent on the substrate and it was coupled to the specific rearrangement of the microfilament characterizing cell death [5].
  • gas2 is a multifunctional gene involved in the regulation of apoptosis and chondrogenesis in the developing mouse limb [6].
 

Anatomical context of Gas2

  • Gas2, a component of the microfilament system, belongs to the class of gas genes whose expression is induced at growth arrest [3].
  • In none of the analyzed oncogene-transformed NIH 3T3 cell lines was Gas2 expression induced under serum starvation [4].
  • Overexpression of Gas2 deleted at its C-terminal region (delta 276-314 and delta 236-314), but not its wild-type form, induces dramatic changes in the actin cytoskeleton and cell morphology [3].
  • Growth arrest-specific (Gas2) protein has been shown to be a component of the microfilament system, that is highly expressed in growth arrested mouse and human fibroblasts and is hyperphosphorylated upon serum stimulation of quiescent cells [7].
  • On the other hand LPA, a specific stimulus for stress fiber formation, fails to induce a detectable Gas2 hyperphosphorylation [7].
 

Associations of Gas2 with chemical compounds

  • RA treatment increased the expression of gas3 and caused gas2 to be transiently overexpressed in amino-acid-deficient medium [8].
  • In the absence of dexamethasone, 3T3-L1 cells underwent mitoses but failed to establish postmitotic growth arrest, as evidenced by the persistence of elevated GAS2 mRNA [9].
 

Other interactions of Gas2

  • This inhibition correlated with the absence of the Gas2 peptide and pro-caspase-3 cleavage [6].
  • There was a higher expression of gas2 protein during exponential growth than during growth arrest, induced either by serum starvation or by TGFbeta treatment [10].
 

Analytical, diagnostic and therapeutic context of Gas2

  • Exactly at these time points, the C-terminal domain of the Gas2 peptide was cleaved as revealed by Western blot analysis [6].

References

  1. The death substrate Gas2 binds m-calpain and increases susceptibility to p53-dependent apoptosis. Benetti, R., Del Sal, G., Monte, M., Paroni, G., Brancolini, C., Schneider, C. EMBO J. (2001) [Pubmed]
  2. Microtubule actin cross-linking factor (MACF): a hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons. Leung, C.L., Sun, D., Zheng, M., Knowles, D.R., Liem, R.K. J. Cell Biol. (1999) [Pubmed]
  3. Microfilament reorganization during apoptosis: the role of Gas2, a possible substrate for ICE-like proteases. Brancolini, C., Benedetti, M., Schneider, C. EMBO J. (1995) [Pubmed]
  4. Gas2, a growth arrest-specific protein, is a component of the microfilament network system. Brancolini, C., Bottega, S., Schneider, C. J. Cell Biol. (1992) [Pubmed]
  5. Caspase-3 and caspase-7 but not caspase-6 cleave Gas2 in vitro: implications for microfilament reorganization during apoptosis. Sgorbissa, A., Benetti, R., Marzinotto, S., Schneider, C., Brancolini, C. J. Cell. Sci. (1999) [Pubmed]
  6. gas2 is a multifunctional gene involved in the regulation of apoptosis and chondrogenesis in the developing mouse limb. Lee, K.K., Tang, M.K., Yew, D.T., Chow, P.H., Yee, S.P., Schneider, C., Brancolini, C. Dev. Biol. (1999) [Pubmed]
  7. Phosphorylation of the growth arrest-specific protein Gas2 is coupled to actin rearrangements during Go-->G1 transition in NIH 3T3 cells. Brancolini, C., Schneider, C. J. Cell Biol. (1994) [Pubmed]
  8. Effects of nutrient deprivation and differentiation on the expression of growth-arrest genes (gas and gadd) in F9 embryonal carcinoma cells. Fleming, J.V., Hay, S.M., Harries, D.N., Rees, W.D. Biochem. J. (1998) [Pubmed]
  9. Dexamethasone signaling is required to establish the postmitotic state of adipocyte development. Shugart, E.C., Umek, R.M. Cell Growth Differ. (1997) [Pubmed]
  10. Expression of growth arrest-specific (Gas) genes in murine keratinocytes: Gas2 is specifically regulated. Manzow, S., Brancolini, C., Marks, F., Richter, K.H. Exp. Cell Res. (1996) [Pubmed]
 
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