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The mitogen activated protein kinase (MAPK) family of proteins is involved inregulating cellular fate activities such as proliferation, differentiation andapoptosis. Their fundamental importance has attracted considerable attention ondifferent aspects of the MAPK signaling dynamics; this is particularly true forthe Erk/Mek system, which has become the canonical example for MAPK signalingsystems. Erk exists in many different isoforms, of which the most widelystudied are Erk1 and Erk2. Until recently, these two kinases were consideredequivalent as they differ only subtly at the sequence level; however, theseisoforms exhibit radically different trafficking between cytoplasm and nucleus.Here we use spatially resolved data on Erk1/2 to develop and analyzespatio-temporal models of these cascades; and we discuss how sensitivityanalysis can be used to discriminate between mechanisms. We are especiallyinterested in understanding why two such similar proteins should co-exist inthe same organism, as their functional roles appear to be different. Our modelselucidate some of the factors governing the interplay between processes and theErk1/2 localization in different cellular compartments, including competitionbetween isoforms. This methodology is applicable to a wide range of systems,such as activation cascades, where translocation of species occurs via signalpathways. Furthermore, our work may motivate additional emphasis forconsidering potentially different roles for isoforms that differ subtly at thesequence level.

Dependence of MAPK mediated signaling on Erk isoforms and differences in nuclear shuttling