The cytochrome c oxidase-cytochrome c complex: spectroscopic analysis of conformational changes in the protein-protein interaction domain

Biochemistry ◽  
1989 ◽  
Vol 28 (2) ◽  
pp. 456-462 ◽  
Author(s):  
Bruno Michel ◽  
Amanda E. I. Proudfoot ◽  
Carmichael J. A. Wallace ◽  
Hans Rudolf Bosshard
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Conformational Changes ◽  
Protein Interaction ◽  
Spectroscopic Analysis ◽  
Interaction Domain ◽  
Protein Protein Interaction ◽  
C Complex

scholarly journals Complex structure of cytochrome c –cytochrome c  oxidase reveals a novel protein–protein interaction mode

2016 ◽  
Vol 36 (3) ◽  
pp. 291-300 ◽  
Author(s):  
Satoru Shimada ◽  
Kyoko Shinzawa‐Itoh ◽  
Junpei Baba ◽  
Shimpei Aoe ◽  
Atsuhiro Shimada ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Protein Interaction ◽  
Complex Structure ◽  
Protein Protein Interaction ◽  
Interaction Mode ◽  
Novel Protein

scholarly journals Regulation of clathrin coat assembly by Eps15 homology domain–mediated interactions during endocytosis

2012 ◽  
Vol 23 (4) ◽  
pp. 687-700 ◽  
Author(s):  
Ryohei Suzuki ◽  
Junko Y. Toshima ◽  
Jiro Toshima
Keyword(s):  
Functional Diversity ◽  
Protein Interaction ◽  
Interaction Domain ◽  
Protein Protein Interaction ◽  
Molecular Events ◽  
Biological Studies ◽  
Eh Domain ◽  
Actin Patch ◽  
Lines Of Evidence

Clathrin-mediated endocytosis involves a coordinated series of molecular events regulated by interactions among a variety of proteins and lipids through specific domains. One such domain is the Eps15 homology (EH) domain, a highly conserved protein–protein interaction domain present in a number of proteins distributed from yeast to mammals. Several lines of evidence suggest that the yeast EH domain–containing proteins Pan1p, End3p, and Ede1p play important roles during endocytosis. Although genetic and cell-biological studies of these proteins suggested a role for the EH domains in clathrin-mediated endocytosis, it was unclear how they regulate clathrin coat assembly. To explore the role of the EH domain in yeast endocytosis, we mutated those of Pan1p, End3p, or Ede1p, respectively, and examined the effects of single, double, or triple mutation on clathrin coat assembly. We found that mutations of the EH domain caused a defect of cargo internalization and a delay of clathrin coat assembly but had no effect on assembly of the actin patch. We also demonstrated functional redundancy among the EH domains of Pan1p, End3p, and Ede1p for endocytosis. Of interest, the dynamics of several endocytic proteins were differentially affected by various EH domain mutations, suggesting functional diversity of each EH domain.

scholarly journals Classification of Nonenzymatic Homologues of Protein Kinases

2009 ◽  
Vol 2009 ◽  
pp. 1-17 ◽  
Author(s):  
K. Anamika ◽  
K. R. Abhinandan ◽  
K. Deshmukh ◽  
N. Srinivasan
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Protein Interaction ◽  
Transmembrane Domain ◽  
Homo Sapiens ◽  
Interaction Domain ◽  
Protein Protein Interaction ◽  
Domain 3 ◽  
Eukaryotic Organisms ◽  
And Function

Protein Kinase-Like Non-kinases (PKLNKs), which are closely related to protein kinases, lack the crucial catalytic aspartate in the catalytic loop, and hence cannot function as protein kinase, have been analysed. Using various sensitive sequence analysis methods, we have recognized 82 PKLNKs from four higher eukaryotic organisms, namely,Homo sapiens,Mus musculus,Rattus norvegicus, andDrosophila melanogaster. On the basis of their domain combination and function, PKLNKs have been classified mainly into four categories: (1) Ligand binding PKLNKs, (2) PKLNKs with extracellular protein-protein interaction domain, (3) PKLNKs involved in dimerization, and (4) PKLNKs with cytoplasmic protein-protein interaction module. While members of the first two classes of PKLNKs have transmembrane domain tethered to the PKLNK domain, members of the other two classes of PKLNKs are cytoplasmic in nature. The current classification scheme hopes to provide a convenient framework to classify the PKLNKs from other eukaryotes which would be helpful in deciphering their roles in cellular processes.

scholarly journals A Novel and Conserved Protein-Protein Interaction Domain of Mammalian Lin-2/CASK Binds and Recruits SAP97 to the Lateral Surface of Epithelia

2002 ◽  
Vol 22 (6) ◽  
pp. 1778-1791 ◽  
Author(s):  
Seonok Lee ◽  
Shuling Fan ◽  
Olya Makarova ◽  
Samuel Straight ◽  
Ben Margolis
Keyword(s):  
Protein Interaction ◽  
Protein Interactions ◽  
Mdck Cells ◽  
Cell Polarization ◽  
Dominant Negative ◽  
Mammalian Development ◽  
Interaction Domain ◽  
Membrane Recruitment ◽  
Protein Protein Interaction ◽  
N Terminus

ABSTRACT Mammalian Lin-2 (mLin-2)/CASK is a membrane-associated guanylate kinase (MAGUK) and contains multidomain modules that mediate protein-protein interactions important for the establishment and maintenance of neuronal and epithelial cell polarization. The importance of mLin-2/CASK in mammalian development is demonstrated by the fact that mutations in mLin-2/CASK or SAP97, another MAGUK protein, lead to cleft palate in mice. We recently identified a new protein-protein interaction domain, called the L27 domain, which is present twice in mLin-2/CASK. In this report, we further define the binding of the L27C domain of mLin-2/CASK to the L27 domain of mLin-7 and identify the binding partner for L27N of mLin-2/CASK. Biochemical analysis reveals that this L27N domain binds to the N terminus of SAP97, a region that was previously reported to be essential for the lateral membrane recruitment of SAP97 in epithelia. Our colocalization studies, using dominant-negative mLin-2/CASK, show that the association with mLin-2/CASK is crucial for lateral localization of SAP97 in MDCK cells. We also report the identification of a novel isoform of Discs Large, a Drosophila melanogaster orthologue of SAP97, which contains a region highly related to the SAP97 N terminus and which binds Camguk, a Drosophila orthologue of mLin-2/CASK. Our data identify evolutionarily conserved protein-protein interaction domains that link mLin-2/CASK to SAP97 and account for their common phenotype when mutated in mice.

scholarly journals Divergent evolution of a protein-protein interaction revealed through ancestral sequence reconstruction and resurrection

2020 ◽  
Author(s):  
Louise Laursen ◽  
Jelena Čalyševa ◽  
Toby J. Gibson ◽  
Per Jemth
Keyword(s):  
Protein Interaction ◽  
Postsynaptic Density ◽  
Ancestral Sequence ◽  
Scaffolding Protein ◽  
Divergent Evolution ◽  
Last Common Ancestor ◽  
Interaction Domain ◽  
Protein Protein Interaction ◽  
Ancestral Sequence Reconstruction ◽  
Sequence Reconstruction

AbstractThe postsynaptic density extends across the postsynaptic dendritic spine with Discs large (DLG) as the most abundant scaffolding protein. DLG dynamically alters the structure of the postsynaptic density, thus controlling the function and distribution of specific receptors at the synapse. PDZ domains make up one of the most abundant protein interaction domain families in animals. One important interaction governing postsynaptic architecture is that between the PDZ3 domain from DLG and cysteine-rich interactor of PDZ3 (CRIPT). However, little is know regarding functional evolution of the PDZ3:CRIPT interaction. Here, we subjected PDZ3 and CRIPT to ancestral sequence reconstruction, resurrection and biophysical experiments. We show that the PDZ3:CRIPT interaction is an ancient interaction, which was present in the last common ancestor of Eukaryotes, and that high affinity is maintained in most extant animal phyla. However, affinity is low in nematodes and insects, raising questions about the physiological function of the interaction in species from these animal groups. Our findings demonstrate how an apparently established protein-protein interaction involved in cellular scaffolding in bilaterians can suddenly be subject to dynamic evolution including possible loss of function.

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