Annual Review of Biochemistry
Vol. 44:147-159 (Volume publication date July 1975)
https://doi.org/10.1146/annurev.bi.44.070175.001051
Shenghong Ma, Zhipeng Meng, Rui Chen, Kun-Liang Guan
Vol. 88, 2019
The Hippo pathway was initially discovered in Drosophila melanogaster as a key regulator of tissue growth. It is an evolutionarily conserved signaling cascade regulating numerous biological processes, including cell growth and fate decision, organ size ...Read More
Figure 1: Core components of the Hippo pathway in mammalian cells. The Hippo pathway activity controls the dynamic localization of YAP/TAZ between nucleus and cytoplasm. (a) When the Hippo pathway is ...
Figure 2: Mechanical cues regulate YAP/TAZ activities through Rho GTPase and the Hippo pathway. Cell–cell contact, cell stretching, cell tension, extracellular matrix (ECM) stiffness, and changes in c...
Figure 3: The Hippo pathway integrates multiple signals to regulate the activity of YAP/TAZ. The LATS kinase activity is controlled by cell polarity and cell adhesion through KIBRA/NF2, tight junction...
Figure 4: YAP/TAZ and cancer hallmarks. The Hippo pathway effectors YAP/TAZ directly or indirectly control multiple cancer hallmarks, including proliferation, survival, evading growth suppressors, rep...
Haifeng Wang, Marie La Russa, Lei S. Qi
Vol. 85, 2016
The Cas9 protein (CRISPR-associated protein 9), derived from type II CRISPR (clustered regularly interspaced short palindromic repeats) bacterial immune systems, is emerging as a powerful tool for engineering the genome in diverse organisms. As an RNA-...Read More
Figure 1: CRISPR-associated protein 9 (Cas9)-mediated sequence-specific genomic editing. (a) Comparison of programmable sequence-specific genome editing nucleases. (Top) Zinc-finger nucleases (ZFNs) a...
Figure 2: Nuclease-deactivated Cas9 (dCas9)-mediated sequence-specific gene regulation. (a) CRISPR interference (CRISPRi) strategies. Repression can occur with dCas9 alone in bacteria, which stericall...
Figure 3: Applications of CRISPR-associated protein 9 (Cas9) in gene editing, gene regulation, epigenome editing, and genomic imaging. (a) Cas9-mediated site-specific genome editing has a variety of a...
Nils Wiedemann and Nikolaus Pfanner
Vol. 86, 2017
Mitochondria are essential organelles with numerous functions in cellular metabolism and homeostasis. Most of the >1,000 different mitochondrial proteins are synthesized as precursors in the cytosol and are imported into mitochondria by five transport ...Read More
Figure 1: Overview of the five major protein import pathways of mitochondria. Presequence-carrying preproteins are imported by the translocase of the outer mitochondrial membrane (TOM) and the presequ...
Figure 2: The presequence pathway into the mitochondrial inner membrane (IM) and matrix. The translocase of the outer membrane (TOM) consists of three receptor proteins, the channel-forming protein To...
Figure 3: Role of the oxidase assembly (OXA) translocase in protein sorting. Proteins synthesized by mitochondrial ribosomes are exported into the inner membrane (IM) by the OXA translocase; the ribos...
Figure 4: Carrier pathway into the inner membrane. The precursors of the hydrophobic metabolite carriers are synthesized without a cleavable presequence. The precursors are bound to cytosolic chaperon...
Figure 5: Mitochondrial intermembrane space import and assembly (MIA) machinery. Many intermembrane space (IMS) proteins contain characteristic cysteine motifs. The precursors are kept in a reduced an...
Figure 6: Biogenesis of β-barrel proteins of the outer mitochondrial membrane. The precursors of β-barrel proteins are initially imported by the translocase of the outer membrane (TOM), bind to small ...
Figure 7: The dual role of mitochondrial distribution and morphology protein 10 (Mdm10) in protein assembly and organelle contact sites. Mdm10 associates with the sorting and assembly machinery (SAM) ...
Figure 8: Multiple import pathways for integral α-helical proteins of the mitochondrial outer membrane. The precursors of proteins with an N-terminal signal anchor sequence are typically inserted into...
Figure 9: The mitochondrial contact site and cristae organizing system (MICOS) interacts with protein translocases. MICOS consists of two core subunits, Mic10 and Mic60. Mic10 forms large oligomers th...
Peter B. Moore and Thomas A. Steitz
Vol. 72, 2003
▪ Abstract The ribosome crystal structures published in the past two years have revolutionized our understanding of ribonucleoprotein structure, and more specifically, the structural basis of the peptide bonding forming activity of the ribosome. This ...Read More
Figure 1: The appearance of the large ribosomal subunit from H. marismortui in electron density maps at different resolutions. The subunit is shown in the crown view at (a) 9 Å resolution (46), (b) 5...
Figure 1: The appearance of the large ribosomal subunit from H. marismortui in electron density maps at different resolutions. The subunit is shown in the crown view at (a) 9 Å resolution (46), (b) 5...
Figure 2: The structure of kink-turn 7 in the 23s rRNA of the H. marismortui ribosome. (a) The secondary structure of KT-7. The C-stem is red, the NC-stem blue, and the bulged nucleotide is green. (b...
Figure 3: The A-minor motif. (a) Examples of the three most important kinds of A-minor motifs from the 23S rRNA of H. marismortui. Types I and II are A-specific. Type III interactions involving other...
Figure 4: A space filling model of the large ribosomal subunit from H. marismortui with a transition state analog bound viewed down the active site cleft. Bases are white, the sugar-phosphate backbon...
Figure 5: Ribosomal proteins in the H. marismortui large ribosomal subunit. (a) A ribbon representation of L15 (yellow) and the RNA sequences with which it interacts (red). The globular domain of the...
Figure 5: Ribosomal proteins in the H. marismortui large ribosomal subunit. (a) A ribbon representation of L15 (yellow) and the RNA sequences with which it interacts (red). The globular domain of the...
Figure 6: A ribosome-catalyzed peptide bond forming reaction involving low mol wt substrates. The reaction of CCA-phenylalanine-caproic acid-biotin (CCA-pcb) and C-puromycin (C-pmn) that yields CCA a...
Figure 7: The structure of the large ribosomal subunit from H. marismortui with products of the fragment reaction (CCA and C-pmn-pcb: see Figure 6) bound in the peptidyl transferase center. (a) A spa...
Figure 8: Steps in the peptidyl transferase reaction pathway. (a) The superposition of two independently determined cocrystal structures suggests that the α-amino group of an A-site substrate is posi...
Figure 9: The interaction of macrolide antibiotics with the large ribosomal subunit of H. marismortui. (a) A superposition of several macrolides/large ribosomal subunit complex structures. Structures...
Figure 10: Antibiotic structures and antibiotic interactions with the H. marismortui large ribosomal subunit. (a) The structures of two macrolide antibiotics. (b) The interactions of sparsomycin (gre...
D. Michiel Pegtel and Stephen J. Gould
Vol. 88, 2019
Exosomes are small, single-membrane, secreted organelles of ∼30 to ∼200 nm in diameter that have the same topology as the cell and are enriched in selected proteins, lipids, nucleic acids, and glycoconjugates. Exosomes contain an array of membrane-...Read More
Figure 1: Exosomes are heterogeneous in size, heterogeneous in composition, and enriched in membrane-associated, high-order oligomeric protein complexes. Although it is likely that no exosome contains...
Figure 2: Exosomes bud from endosome and plasma membranes. Exosome biogenesis occurs by three modes: () vesicle budding into discrete endosomes that mature into multivesicular bodies, which release ex...
