Organizations should know their people: a behavioral economics approach

Public and private organizations are increasingly applying behavioral economics methods to a variety of issues such as mechanism design and incentive architecture. However, there has been little focus on how experimental tools used in behavioral economics can help companies learn more about their (current or prospective) workforce and, more specifically, about their employees’ tastes and inclinations. This has important implications for broader organizational performance since some designs/incentives are likely to affect only individuals with a particular disposition (e.g. risk averse or fairness oriented) but not others, or can even have opposite effects on individuals with different sets of preferences. In this commentary, we point out a number of promising avenues for the application of a behavioral economics lens to understand and manage people within organizations. A comprehensive case study is also provided

Conservation and consensus pattern of the IYT motif of yeast MKPs.

<p>(A) Dendrogram of <i>S. cerevisiae</i> (Sc) full sequences of genes encoding MKPs Msg5 and Sdp1 and the orthologous sequences from the indicated yeast species. (B) ClustalW multiple sequence alignment of the region containing the IYT motif within MKPs from <i>Saccharomyces kudriavzevii</i> (Sk), <i>Saccharomyces arboricola</i> (Sa), <i>Naumovozyma dairenensis</i> (Nd), <i>Naumovozyma castellii</i> (Nc), <i>Torulaspora delbrueckii</i> (Td), <i>Kazachstania naganishii</i> (Kn), <i>Vanderwaltozyma polyspora</i> (Vp), <i>Zygosaccharomyces rouxii</i> (Zr), <i>Ashbya gossypii</i> (Ag), <i>Kluyveromyces lactis</i> (Kl) <i>Candida glabrata</i> (Cg), <i>Schizosaccharomyces pombe</i> (Sp) and <i>Eremothecium cymbalariae</i> (Ec). Dendrogram was created with the software Mega 5.2. Conserved residues are dotted while identical residues are labelled with asterisks. (C) Consensus pattern and sequence logo of the IYT motif generated by the NEME software <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0085390#pone.0085390-Bailey1" target="_blank">[38]</a>. The overall height of each stack indicates the sequence conservation at that position (measured in bits), whereas the height of symbols within the stack reflects the relative frequency of the corresponding amino acid at that position.</p

Effect of the lack of the IYT motif of inactive Msg5 on MAPK trapping.

<p>(A) Western blotting analysis of the wild type strain YPH499 bearing YEp352GST (vector), YEp352MSG5GST (Msg5), YEp352MSG5^C319AGST (Msg5^C319A) or YEp352MSG5^C319A-IAYATAGST (Msg5^C319A-IAYATA) plasmids. Cells were grown to mid-log phase at 24°C and then aliquots were treated or not with Congo red (30 µg/ml) for 180 min. Protein extracts were prepared and phosphorylated MAPKs (Slt2, Kss1 and Fus3), Msg5-GST and G6PDH (as a loading control) were detected with anti-phospho-p42/44 (two upper panels), anti-GST antibody (middle panel) and anti-G6PDH antibodies (lower panel), respectively. (B) Expression of <i>MLP1-GFP</i> was examined by determining GFP signal in the same transformants (additionally carrying <i>pMLP1</i>-<i>GFP</i> plasmid) and growth conditions as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0085390#pone-0085390-g004" target="_blank">Figure 4A</a>. Data shown are the average of three independent experiments performed in duplicate. Error bars indicate standard deviations. (C) Upper panels: Western blotting analysis of the <i>msg5Δ</i> mutant strain DD1-2D, carrying the same plasmids as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0085390#pone-0085390-g004" target="_blank">Figure 4A</a>. Lower panels: sensitivity to Congo red of the same transformants as above. Cells were grown in liquid selective medium at 24°C, and a 10-fold dilution series of this culture was spotted onto YPD agar medium in the absence (no stress) or presence of Congo Red (75 µg/ml) and incubated for 2 days at 24°C. Similar results were obtained in three different experiments and selected images correspond to representative blots.</p

Effect of the lack of the IYT motif of Sdp1 on the CWI pathway.

<p>(A) Western blotting analysis of the Y00897 (<i>gas1</i>Δ) strain transformed with pYES2 (vector), pYES2SDP1myc (Sdp1), pYES2SDP1^IAYATAmyc (Sdp1^IAYATA), pYES2SDP1^C140A (Sdp1^C140A) or pYES2SDP1^C140A-IAYATA (Sdp1^C140A-IAYATA) plasmids. Cells were cultured to mid-log phase in raffinose-based selective medium at 24°C, then galactose was added to a final 2% concentration for 4 hours at 24°C, and protein extracts were prepared. Phospho-Slt2, Sdp1-Myc and G6PDH (as a loading control) were detected with anti-phospho-p42/44 (upper panel), anti-Myc (middle panel) and anti-G6PDH (lower panel) antibodies, respectively. (B) Expression of <i>MLP1-lacZ</i> was examined by determining β-galactosidase activity in cell extracts of the same transformants as in <i>A</i> also carrying the <i>pMLP1</i>-LACZ plasmid. Data shown are the average of three independent experiments performed in duplicate. Error bars indicate standard deviations. (C) Western blotting analysis of the wild type YPH499 strain transformed with the same plasmids as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0085390#pone-0085390-g002" target="_blank">Figure 2A</a>. Cell growth conditions, extract preparation and immunoblot analysis was performed as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0085390#pone-0085390-g002" target="_blank">Figure 2A</a>. (D) <i>In vivo</i> localisation of Slt2-GFP in YPH499 yeast cells carrying the plasmid pRS425-<i>SLT2</i>-GFP transformed with pYES2 (vector), pYES2SDP1^C140A (Sdp1^C140A) or pYES2SDP1^C140A-IAYATA (Sdp1^C140A-IAYATA) plasmids. Cells were grown to mid-log phase in raffinose-based selective medium at 24°C, and then galactose was added to a final 2% concentration for 4 hours at 24°C. Fluorescence microscopy photographs showing the cellular distribution of the fluorescent Slt2-GFP were taken. Bars, 5 µm. The percentage of cells showing nuclear accumulation of Slt2-GFP from the same cultures was determined. Data shown are the average of three independent experiments in which n>100. Error bars indicate standard deviations (E) Western blotting analysis of the WT BY4741 strain transformed with pYES2 (vector), pYES2SDP1^C140A (Sdp1^C140A), pYES2SDP1^C140A-IAYATA (Sdp1^C140A-IAYATA), pYES2SDP1^C140A-IA (Sdp1^C140A-IA), pYES2SDP1^C140A-YA (Sdp1^C140A-YA) or pYES2SDP1^C140A-TA (Sdp1^C140A-TA) plasmids. Cells were cultured and extracts processed as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0085390#pone-0085390-g003" target="_blank">Figure 3A</a>. Similar results were obtained in three different experiments and selected images correspond to representative blots.</p

Conserved IYT motif participates in binding of Pmp1 phosphatase to Pmk1 MAPK in <i>S. pombe</i>.

<p>(A) Strains MI200 (Pmk1-HA6H; Control), MI212 (<i>pmp1Δ</i>, Pmk1-HA6H), DP400 (<i>pmp1Δ, pmp1-GST, pmk1-HA6H</i>), and DP420 (<i>pmp1Δ, pmp1(I10A Y11A T12A)-GST, pmk1-HA6H</i>) were grown in YES medium to early-log phase, extracts were prepared and Pmk1-HA6H was purified by affinity chromatography. Phosphorylated Pmk1 was detected by immunoblotting with anti-phosho-p42/44 antibody (upper panel), total Pmk1 with anti-HA antibody as loading control (middle panel), and total Pmp1 with anti-GST antibody. (B) Ten-fold dilution series of cultures from strains MI212, DP400 and DP420 were spotted on YES plates or YES plates supplemented with either 0.3, 0.4 and 0.5 M MgCl₂, and incubated for 3 days at 28°C. (C) Strains MI200 (control, lane 1), DP410 (<i>pmp1Δ, pmp1(C158S)-GST, pmk1-HA6H</i>; lane 2) and DP430 (<i>pmp1Δ, pmp1(I10A Y11A T12A C158S)-GST, pmk1-HA6H</i>; lane 3) were grown in YES medium to early-log phase, extracts were prepared and Pmp1-GST fusions were recovered after incubation with glutathione(GSH)-agarose beads. After extensive washes, the bound proteins were detected by immunoblotting with anti-HA (upper panel) and anti-GST antibodies (middle panel). Total extracts from the above strains were probed with anti-HA antibody as a loading control (lower panel). (D) Strains MI200 (Control), MI212 (<i>pmp1Δ</i>), DP400 (<i>pmp1-GST</i>), DP410 (<i>pmp1(C158S)-GST</i>) and DP430 (<i>pmp1(I10A Y11A T12A C158S)-GST</i>) were grown in YES medium to early-log phase, extracts were prepared and Pmk1-HA6H was purified by affinity chromatography. Immunodetection was performed as in A. Similar results were obtained in three different experiments and selected images correspond to representative blots.</p

Involvement of the Sdp1 IYT motif on Slt2 and Mlp1 binding.

<p>(A) Western blotting analysis of <i>in vivo</i> co-purification of Sdp1 with Slt2. Cell extracts of the wild type strain YPH499 transformed with plasmids YCplac22Sdp1m (Sdp1) or YCplac22Sdp1^IAYATAm (Sdp1^IAYATA) and plasmids pEG(KG) (GST) or pEG(KG)-SLT2 (Slt2) were incubated with glutathione-Sepharose to pull-down GST-complexes. Immunodetection was performed with anti-Myc (upper panel) and anti-GST (lower panel) antibodies. (B) Western blotting analysis of <i>in vitro</i> co-purification of recombinant Sdp1 with recombinant Slt2. <i>E. coli</i> extracts containing GST, GST-Sdp1 or GST-Sdp1^IAYATA were mixed with <i>E. coli</i> extracts containing Slt2-His and then incubated with glutathione-Sepharose to pull-down GST-complexes. Immunodetection was performed using anti-polyHis (upper panel) and anti-GST (lower panel) antibodies. (C) Western blotting analysis of <i>in vivo</i> co-purification of Sdp1 with Mlp1. Cell extracts of the strain YPH499 transformed with plasmids YCplac22Sdp1m (Sdp1) or YCplac22Sdp1IAYATAm (Sdp1^IAYATA) and plasmids pEG(KG) (GST) or pEG(KG)-MLP1 (Mlp1), were processed as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0085390#pone-0085390-g001" target="_blank">Figure 1B</a>. (D) Western blotting analysis of <i>in vitro</i> co-purification of recombinant Sdp1 with recombinant Mlp1. Experiments were performed as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0085390#pone-0085390-g001" target="_blank">Figure 1C</a> but using <i>E. coli</i> extracts containing Mlp1-His. Similar results were obtained in three different experiments and selected images correspond to representative blots.</p

Rho1 is involved in Pmk1 activation in response to cell wall stress.

<p>Strains MI200 (<i>pmk1-HA6H</i>, WT), LS201 (<i>rho1-596</i>), MI700 (<i>rho2Δ</i>), and LS202 (<i>rho1-596 rho2Δ</i>) were grown in YES medium to mid log-phase, and treated with (A) 0.6 M KCl, (B) 1 mM H₂O₂, or (C) 1 µg/ml Caspofungin. At different times Pmk1-HA6H was purified and both activated and total Pmk1 were detected by immunoblotting with anti-phospho-p42/44 and anti-HA antibodies, respectively. (D) Rho1 and Pmk1 play additive roles in cell survival during cell wall stress. Strains MI200 (WT), MI700 (<i>rho2Δ</i>), GB3 (<i>pck2Δ</i>), GB29 (<i>rho2Δ pck2Δ</i>), LS201 (<i>rho1-596</i>), LS202 (<i>rho1-596 rho2Δ</i>), LS203 (<i>rho1-596 pck2Δ</i>), MI102 (<i>pmk1Δ</i>) and LS209 (<i>rho1-596 pmk1Δ</i>) were grown in YES medium, and 10⁴, 10³, 10² and 10 cells were spotted onto YES plates supplemented with increased concentrations of Caspofungin. The plates were incubated for 4 days at 28°C before being photographed.</p

<i>S. pombe</i> strains.

a<p>All strains are <i>ade- ura4D-18 leu1-32</i>.</p