This study takes a dynamic multilevel approach to examine how the relationship between an employee's job satisfaction trajectory and subsequent turnover may change depending on the employee's unit's job satisfaction trajectory and its dispersion. Analyses of longitudinal multilevel data collected from 5,270 employees in 175 business units of a hospitality company demonstrate a significant three-way interactive effect of unit-level job satisfaction trajectory and its dispersion and individual job satisfaction trajectory on individual job exit. In particular, in the presence of a negative unit-level job satisfaction trajectory and low dispersion, a positive change in individual-level job satisfaction does not affect the odds of a person leaving an organization.Put differently, an employee's being out of step with prevailing unit-level attitudes appears to alter the relationship between his or her job satisfaction trajectory and turnover propensity. Further, unit-level job-satisfaction change and its dispersion jointly influence the overall turnover rate in a unit. The results indicate unit-level and individual-level job satisfaction trajectories have unique multilevel influences on turnover above and beyond static levels of job satisfaction. Accounting for these dynamics substantially increases the explained variance in turnover behavior. The findings increase understanding of the job satisfaction-turnover link over time and across levels.

Alkaline phosphatase (ALP)-catalyzed hydrogelation has been extensively explored and found wide applications. Spectroscopic and electrochemical approaches are commonly employed for the detection of ALP activity. Herein, by rational design of a fluorescence probe Fmoc-K(FITC)FFYp (P1) (where FITC is fluorescein), we incorporated sol-gel transition with fluorescence "turn-off" and developed a new method for quantitative sensing ALP activity in vitro and in living cells. Under the catalysis of ALP, P1 was converted to hydrogelator Fmoc-K(FITC)FFY (1) which self-assembles into nanofibers to form Gel I. Accompanying this sol-gel transition, the fluorescence emission of P1 was turned off. Our assay was employed to detect ALP activity over the range of 0-2.8 U/mL with a limit of detection (LOD) of 0.06 U/mL. ALP-inhibitor-treated cell imaging indicated that P1 could be applied for sensing ALP activity in living cells. Our method provides a new option for real time and quantitative sensing ALP activity in vitro and even in living cells.