Society of General Physiologists series最新文献

Dissection of protein kinase and phosphatase targeting interactions. 蛋白激酶和磷酸酶靶向相互作用的解剖。

Society of General Physiologists series Pub Date : 1997-01-01

J D Scott

{"title":"Dissection of protein kinase and phosphatase targeting interactions.","authors":"J D Scott","doi":"","DOIUrl":"","url":null,"abstract":"Protein phosphorylation is a primary means of mediating signal transduction events that control cellular processes. Accordingly, the activities of protein kinases and phosphatases are highly regulated. One level of regulation is that the subcellular distribution of several kinases and phosphatases is restricted by association with targeting proteins or subunits. This mechanism promotes rapid and preferential modulation of specific targets within a defined microenvironment in response to diffusible second messengers. The type II cAMP-dependent protein kinase (PKA) is targeted by association of its regulatory subunit (RII) with A-kinase anchoring proteins (AKAPs). To date, 36 unique AKAPs have been identified. Each of these proteins contains a conserved amphipathic helix responsible for AKAP association with cellular structures. Disruption of PKA/AKAP interaction with peptides patterned after the amphipathic helix region blocks certain cAMP responses, including the modulation of glutamate receptor ion-channel activity in neurons and transcription of cAMP-responsive genes. Yeast two-hybrid screening methods have identified neuronal specific AKAP79-binding proteins including the beta isoform of the phosphatase 2B, calcineurin. Biochemical and immunological studies have confirmed the two-hybrid results and identified additional members of this multienzyme signaling complex, including certain protein kinase C isoforms. These findings are consistent with colocalization of CaN, PKC, and type II PKA by AKAP79 and suggest a novel model for reversible phosphorylation in which the opposing kinase and phosphatase actions are colocalized in a signal transduction complex by association with a common anchor protein.","PeriodicalId":76550,"journal":{"name":"Society of General Physiologists series","volume":"52 ","pages":"227-39"},"PeriodicalIF":0.0,"publicationDate":"1997-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20153921","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Molecular architecture of tight junctions: occludin and ZO-1. 紧密连接的分子结构:occludin和ZO-1。

Society of General Physiologists series Pub Date : 1997-01-01

S Tsukita, M Furuse, M Itoh

引用次数: 0

Syntrophins: modular adapter proteins at the neuromuscular junction and the sarcolemma. 合营养素:神经肌肉连接处和肌膜上的模块化适配蛋白。

Society of General Physiologists series Pub Date : 1997-01-01

S C Froehner, M E Adams, M F Peters, S H Gee

引用次数: 0

A multiple site, side binding model for the interaction of dystrophin with F-actin. 肌营养不良蛋白与f -肌动蛋白相互作用的多位点、侧结合模型。

Society of General Physiologists series Pub Date : 1997-01-01

J M Ervasti, I N Rybakova, K J Amann

引用次数: 0

Specificity of desmosomal plaque protein interactions with intermediate filaments: keeping adhesive junctions segregated. 桥粒体斑块蛋白与中间纤维相互作用的特异性:保持粘附连接分离。

Society of General Physiologists series Pub Date : 1997-01-01

K J Green, E A Bornslaeger, A P Kowalczyk, H L Palka, S M Norvell

引用次数: 0

Intermediate filament linker proteins. 中间丝连接蛋白

Society of General Physiologists series Pub Date : 1997-01-01

E Fuchs, Y Yang, J Dowling, P Kouklis, E Smith, L Guo, Q C Yu

引用次数: 0

A membrane skeleton that clusters nicotinic acetylcholine receptors in muscle. 在肌肉中聚集烟碱乙酰胆碱受体的膜骨架

Society of General Physiologists series Pub Date : 1997-01-01

R J Bloch, G Bezakova, J A Ursitti, D Zhou, D W Pumplin

{"title":"A membrane skeleton that clusters nicotinic acetylcholine receptors in muscle.","authors":"R J Bloch, G Bezakova, J A Ursitti, D Zhou, D W Pumplin","doi":"","DOIUrl":"","url":null,"abstract":"We have presented ultrastructural and semiquantitative immunofluorescence evidence to support the idea that AChR are clustered in rat myotubes by virtue of their ability to associate with a spectrin-based membrane skeleton. Many of the interactions postulated to be involved in the formation of this skeleton, and in the anchoring of AChR to it, must still be examined at the biochemical level, but the overall similarity of this structure to that of the human erythrocyte is already clear. The ability of different members of the spectrin superfamily to associate in various combinations to form distinct plasmalemmal domains provides some exciting hints as to how the surface membrane can be organized efficiently to subserve multiple purposes. One of the challenges of future research will be to learn how innervation regulates the assembly of the membrane skeleton at the developing NMJ, and how this structure is altered as the junction matures. Another will be to learn if the principles of neuromuscular synaptogenesis are relevant to interactions between neurons in the brain, where cells must distinguish between multiple synaptic inputs and assemble synaptic structures at thousands of distinct sites on the neurolemma. Members of the spectrin superfamily have been identified in synaptic structures in the central nervous system (e.g., Carlin et al., 1983; LeVine and Sahyoun, 1986; Malchiodi-Albedi et al., 1993), so much of what we have learned at the neuromuscular junction may be applicable to central synapses.","PeriodicalId":76550,"journal":{"name":"Society of General Physiologists series","volume":"52 ","pages":"177-95"},"PeriodicalIF":0.0,"publicationDate":"1997-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20154549","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Cell signalling and CAM-mediated neurite outgrowth. 细胞信号传导和cam介导的神经突生长。

Society of General Physiologists series Pub Date : 1997-01-01

F S Walsh, K Meiri, P Doherty

{"title":"Cell signalling and CAM-mediated neurite outgrowth.","authors":"F S Walsh, K Meiri, P Doherty","doi":"","DOIUrl":"","url":null,"abstract":"A wide range of molecules promote nerve growth, and these include cell adhesion molecules (CAMs), NCAM, N-cadherin, and the L1 glycoprotein are CAMs that are normally found on both the advancing growth cone and also on cellular substrates, and in general operate via a homophilic binding mechanism. In recent years it has become clear that nerve growth stimulated by these CAMs does not rely on the adhesion function of these molecules, but instead requires that the CAMs activate second messenger cascades in neurons. A large body of evidence supports the hypothesis that homophilic binding of the CAM in the substrate to the CAM in the neuron leads to activation of the neuronal FGF receptor, possibly via a direct interaction in cis between the CAM and the FGF receptor. The consequential activation of PLC gamma is both necessary and sufficient to account for the neurite outgrowth response stimulated by the above three CAMs. Based on the above model, we reasoned that soluble CAMs might also be able to stimulate neurite outgrowth and that such agents might be developed as potential therapeutic agents for stimulating nerve regeneration. To this end we have made soluble chimeric molecules consisting of the extracellular domain of NCAM or L1 fused to the Fc region of human IgG 1. We have found that these molecules can stimulate neurite outgrowth from rat and mouse cerebellar granule cells cultured on a variety of tissue culture substrates and that they do so by activating the FGF receptor signal transduction cascade in the neurons. Consistent with this model, we find that neurons that have their FGF receptor function ablated as a consequence of the expression of dominant negative FGF receptors, no longer respond to the soluble CAM. Downstream targets of CAM function have also been studied. Addition of soluble CAMs to isolated growth cone preparations from mouse or rat brain leads to enhanced phosphorylation of the GAP-43 protein providing a link between the cell surface and the cytoskeleton.","PeriodicalId":76550,"journal":{"name":"Society of General Physiologists series","volume":"52 ","pages":"221-6"},"PeriodicalIF":0.0,"publicationDate":"1997-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20153920","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Roles of the membrane cytoskeleton in protein sorting. 膜细胞骨架在蛋白质分选中的作用。

Society of General Physiologists series Pub Date : 1997-01-01

W J Nelson, K A Beck, P A Piepenhagen

引用次数: 0

Cytoskeletal interactions with glutamate receptors at central synapses. 中枢突触与谷氨酸受体的细胞骨架相互作用。

Society of General Physiologists series Pub Date : 1997-01-01

G L Westbrook, J J Krupp, B Vissel

{"title":"Cytoskeletal interactions with glutamate receptors at central synapses.","authors":"G L Westbrook, J J Krupp, B Vissel","doi":"","DOIUrl":"","url":null,"abstract":"The data presented here are clearly just the beginning of any comprehensive understanding of the set of regulatory and cytoskeletal proteins that interact with membrane receptors in the postsynaptic density. They do, however, indicate that both glutamate channels at central excitatory synapses are involved in complex protein-protein interactions. For example, while NR2A is important for Ca-dependent inactivation of NMDA receptors, studies in several systems suggest that the other major NR2 subunit in hippocampal neurons, NR2B, predominates at critical times during synapse formation. In addition, the COOH terminus of NR2B binds to several novel cytoskeletal proteins. These results provide circumstantial evidence that NR2B may play specific roles in function and localization of receptors at excitatory synapses. The possible role of NR2B in early synaptic function gains additional support from functional data suggesting that NMDA receptors have specific roles during development (Komuro and Rakic, 1993; Rabacchi et al., 1992; Yen et al., 1993). The essential role of NR1 and NR2B in development is graphically demonstrated by the neonatal death of transgenic mice lacking either of these two subunits (Forrest et al., 1994; Kutsuwada et al., 1996) whereas NR2A and NR2C-deficient mice are less severely affected (Sakimura et al., 1995; Ebralidze et al., 1996).","PeriodicalId":76550,"journal":{"name":"Society of General Physiologists series","volume":"52 ","pages":"163-75"},"PeriodicalIF":0.0,"publicationDate":"1997-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20154548","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0