Improving Undergraduate Life Science Education for the Biosciences Workforce: Overcoming the Disconnect between Educators and Industry.

The BioHealth Capital Region (Maryland, Virginia, and Washington, DC; BHCR) is flush with colleges and universities training students in science, technology, engineering, and mathematics disciplines and has one of the most highly educated workforces in the United States. However, current educational approaches and business recruitment tactics are not drawing sufficient talent to sustain the bioscience workforce pipeline. Surveys conducted by the Mid-Atlantic Biology Research and Career Network identified a disconnect between stakeholders who are key to educating, training, and hiring college and university graduates, resulting in several impediments to workforce development in the BHCR: 1) students are underinformed or unaware of bioscience opportunities before entering college and remain so at graduation; 2) students are not job ready at the time of graduation; 3) students are mentored to pursue education beyond what is needed and are therefore overqualified (by degree) for most of the available jobs in the region; 4) undergraduate programs generally lack any focus on workforce development; and 5) few industry-academic partnerships with undergraduate institutions exist in the region. The reality is that these issues are neither surprising nor restricted to the BHCR. Recommendations are presented to facilitate improvement in the preparation of graduates for today's bioscience industries throughout the United States.

A CC-SAM, for coiled coil-sterile α motif, domain targets the scaffold KSR-1 to specific sites in the plasma membrane.

Kinase suppressor of Ras-1 (KSR-1) is an essential scaffolding protein that coordinates the assembly of the mitogen-activated protein kinase (MAPK) module, consisting of the MAPK kinase kinase Raf, the MAPK kinase MEK (mitogen-activated or extracellular signal-regulated protein kinase kinase), and the MAPK ERK (extracellular signal-regulated kinase) to facilitate activation of MEK and thus ERK. Although KSR-1 is targeted to the cell membrane in part by its atypical C1 domain, which binds to phospholipids, other domains may be involved. We identified another domain in KSR-1 that we termed CC-SAM, which is composed of a coiled coil (CC) and a sterile α motif (SAM). The CC-SAM domain targeted KSR-1 to specific signaling sites at the plasma membrane in growth factor-treated cells, and it bound directly to various micelles and bicelles in vitro, indicating that the CC-SAM functioned as a membrane-binding module. By combining nuclear magnetic resonance spectroscopy and experiments in cultured cells, we found that membrane binding was mediated by helix α3 of the CC motif and that mutating residues in α3 abolished targeting of KSR-1 to the plasma membrane. Thus, in addition to the atypical C1 domain, the CC-SAM domain is required to target KSR-1 to the plasma membrane.