The Driftnet Fishery in the Fort Pierce-Port Salerno Area off Southeast Florida

From May through September 1987, observations were made on 38 trips in the driftnet fishery off the Fort Pierce-Port Salerno area off southeast Florida. Of the number and weight of fish landed on observed trips, 91.6 percent consisted of king mackerel, Scomberomorus cavalla, the targeted species. Over 33 species of fishes were observed among the discarded by-catch. The most frequently occurring species in the discards was little tunny, Euthynnus alletteratus, which made up 67.0 percent by number of the discarded by-catch. Total landings for all commercial gear from Saint Lucie and Martin counties (the counties of the study area) increased 516,741 pounds from 1986 to 1987. In 1986, 55 percent of the catch was from handline and 45 percent from driftnet landings. In 1987, 78 percent was from driftnet and 22 percent from handline landings. A comparison of lengths from recreational and commercial landings showed recreationally caught fish to be, on the average, smaller. No marine mammals, birds, or turtles were entangled in the net on observed trips. Data on cost of nets. fuel, and supplies plus the distribution of earnings among the crew were obtained for five driftnet boats

ERp29 Restricts Connexin43 Oligomerization in the Endoplasmic Reticulum

Connexin43 (Cx43) is a gap junction protein that forms multimeric channels that enable intercellular communication through the direct transfer of signals and metabolites. Although most multimeric protein complexes form in the endoplasmic reticulum (ER), Cx43 seems to exit from the ER as monomers and subsequently oligomerizes in the Golgi complex. This suggests that one or more protein chaperones inhibit premature Cx43 oligomerization in the ER. Here, we provide evidence that an ER-localized, 29-kDa thioredoxin-family protein (ERp29) regulates Cx43 trafficking and function. Interfering with ERp29 function destabilized monomeric Cx43 oligomerization in the ER, caused increased Cx43 accumulation in the Golgi apparatus, reduced transport of Cx43 to the plasma membrane, and inhibited gap junctional communication. ERp29 also formed a specific complex with monomeric Cx43. Together, this supports a new role for ERp29 as a chaperone that helps stabilize monomeric Cx43 to enable oligomerization to occur in the Golgi apparatus