The retromer complex

The retromer complex has been conserved throughout evolution as a retrieval agent for a variety of membrane receptors, in order to prevent their delivery to the degradative pathway. The consequence of this is that retromer biology has implications in areas as diverse as Wnt signalling and amyloid plaque accumulation; clearly it is imperative that we improve our understanding of how retromer fulfils its role in these biological processes.     

The anticodon-anticodon complex

Gel electrophoresis has been used to measure the binding between two tRNAs with complementary anticodons, tRNA^Val (Escherichia coli) (anticodon X,A,C) and tRNA^Tyr (E. coli) (anticodon Q,U,A). The association constant K at 0 °C was found to be 4 × 10⁵ m^?1 which is about three orders of magnitude greater than the association constant for tRNA^Tyr (E. coli) binding its trinucleotide codon UAC. The temperature dependence of K suggests that this results from the rigidity of the anticodon loop. tRNA^Tyr (E. coli) binds an order of magnitude more weakly to tRNA^Val (yeast) than to tRNA^Val (E. coli), presumably because it contains the wobble base pair A · I. The relationship between the anticodon-anticodon complex and codon recognition is discussed.     

The SMN complex

The survival of motor neurons (SMN) protein is the product of the disease-determining gene of the neurodegenerative disorder spinal muscular atrophy (SMA). SMN is part of a stable multiprotein complex that is found in all metazoan cells in the cytoplasm and in nuclear Gems. The SMN complex contains, in addition to SMN, at least six other proteins, named Gemins2-7, and plays an essential role in the assembly of the spliceosomal small nuclear ribonucleoproteins (snRNPs). Through its binding to specific sequences in the snRNAs, the SMN complex surveys the correct identity of the target RNAs and facilitates snRNP assembly. Based on its ability to interact with several other protein and RNA components of cellular RNPs, it is likely that the SMN complex functions as an assemblyosome in the formation of diverse RNP particles, some of which may be of particular importance to the motor neuron. A detailed understanding of the cellular roles of the SMN complex may help the development of therapeutic strategies for this neurodegenerative disease.     

The Golgi complex

Summary The ultrastructural arrangement of membranes of the Golgi complex has been characterized in Golgi fractions isolated from rat liver. Procedures for isolation of these fractions have been modified to provide a good yield of Golgi membranes (60 to 70%) with greater than 50-fold purification of sialyl transferase, an enzyme specific for the Golgi complex. The isolated membranes appear well preserved and both the dimensions and appearance of the Golgi complex observed by negative staining and in sections of the isolated membranes correlate well with that in liver sections.The Golgi complex consists of a series of platelike structures, each consisting of a central sac or cisterna from which a network of fine tubules arises. The tubules increase in diameter towards the periphery of the plate and are associated with the formation of vacuoles or secretory vesicles. The structure of the Golgi complex has been related to its role in glycoprotein biosynthesis.     

The human pre-replication complex is an open complex

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The oligodendrocytic junctional complex

Summary The junctional complex of oligodendrocytes was studied by means of different electron microscopical techniques. This complex is composed of the following junctional membrane formations: 1) tight Junctional domains in the oligodendrocytic membrane near the soma of the cells, 2) fasciae occludentes or focal tight junctions on the outer oligodendrocytic loop of myelin and on the outermost myelin membrane, 3) gap junctions of considerable size variations, either on membranes near the soma or on peripheral oligodendrocytic processes, and 4) non-paranodal transverse bands. The different types of oligodendrocytic junctions are discussed in terms of their functional implications.Supported by a grant from the Deutsche Forschungsgemeinschaft (SFB 114 Bionach) to R. DermietzelThe authors are indebted to Mrs. P. Kalweit and Mr. R. Eichner for technical assistance and Mr. A. Stapper for preparing the drawing. We also thank Mr. U. Malewski and Mr. Khing for their help with the English translation     

The nuclear pore complex

Nuclear pore complexes, the conduits for information exchange between the nucleus and cytoplasm, appear broadly similar in eukaryotes from yeast to human. Precisely how nuclear pore complexes regulate macromolecular and ionic traffic remains unknown, but recent advances in the identification and characterization of components of the complex by proteomics and genomics have provided new insights.