Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton.

Lila, Thomas; Drubin, David G.

doi:10.1091/mbc.8.2.367

Cited by 164 publications

(228 citation statements)

References 78 publications

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“…On the basis of the intracellular localization of DBN-1 and on a tentative functional comparison with its relatives, DBN-1 could furthermore modulate the plasticity and function of postsynaptic sites of neuromuscular junctions, analogous to mAbp1 and drebrin, which are known as essential players in both neurological [43][44][45]28 and immunological 30,29 synapses. In addition, DBN-1 may be involved in vesicle transport, similar to yeast and mammalian Abp1 homologues, which are well-described key regulators of receptor-mediated endocytosis, vesicle trafficking and endocytic structure disassembly [46][47][48][49]32 .…”

Section: Discussionmentioning

confidence: 99%

Drebrin-like protein DBN-1 is a sarcomere component that stabilizes actin filaments during muscle contraction

et al. 2015

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Actin filament organization and stability in the sarcomeres of muscle cells are critical for force generation. Here we identify and functionally characterize a Caenorhabditis elegans drebrin-like protein DBN-1 as a novel constituent of the muscle contraction machinery. In vitro, DBN-1 exhibits actin filament binding and bundling activity. In vivo, DBN-1 is expressed in body wall muscles of C. elegans. During the muscle contraction cycle, DBN-1 alternates location between myosin-and actin-rich regions of the sarcomere. In contracted muscle, DBN-1 is accumulated at I-bands where it likely regulates proper spacing of a-actinin and tropomyosin and protects actin filaments from the interaction with ADF/cofilin. DBN-1 loss of function results in the partial depolymerization of F-actin during muscle contraction. Taken together, our data show that DBN-1 organizes the muscle contractile apparatus maintaining the spatial relationship between actin-binding proteins such as a-actinin, tropomyosin and ADF/cofilin and possibly strengthening actin filaments by bundling.

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Section: Discussionmentioning

confidence: 99%

Drebrin-like protein DBN-1 is a sarcomere component that stabilizes actin filaments during muscle contraction

et al. 2015

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“…The null mutation of the yeast homologue of Abp1, Abp1p, resulted in defects similar to those seen in Rvs167/amphiphysin mutation, including sporulation and reduced viability under certain suboptimal growth conditions. Double mutations in ABP1 and RVS167/amphiphysin genes or one of the genes encoding other cytoskeletal components were genetic lethal (47). In mammalian cells, Abp1 has been shown to be essential for Tf internalization (33,40) and synaptic vesicle recycling (39).…”

Section: Discussionmentioning

confidence: 99%

“…In this study, we showed that Abp1 was required for efficient BCR-mediated Ag internalization, further demonstrating an essential role for Abp1 in endocytosis. Previous studies have shown that Abp1 interacts directly with proteins of the endocytic machinery, including rvs167/amphiphysin in yeast (47) and dynamin in mammalian cells (33). Both amphiphysin and dynamin are important for the membrane fission step of endocytosis (38,48).…”

Section: Discussionmentioning

confidence: 99%

Actin-Binding Protein 1 Regulates B Cell Receptor-Mediated Antigen Processing and Presentation in Response to B Cell Receptor Activation

Onabajo

Seeley

Kale

et al. 2008

The Journal of Immunology

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The BCR serves as both signal transducer and Ag transporter. Binding of Ags to the BCR induces signaling cascades and Ag processing and presentation, two essential cellular events for B cell activation. BCR-initiated signaling increases BCR-mediated Ag-processing efficiency by increasing the rate and specificity of Ag transport. Previous studies showed a critical role for the actin cytoskeleton in these two processes. In this study, we found that actin-binding protein 1 (Abp1/HIP-55/SH3P7) functioned as an actin-binding adaptor protein, coupling BCR signaling and Ag-processing pathways with the actin cytoskeleton. Gene knockout of Abp1 and overexpression of the Src homology 3 domain of Abp1 inhibited BCR-mediated Ag internalization, consequently reducing the rate of Ag transport to processing compartments and the efficiency of BCR-mediated Ag processing and presentation. BCR activation induced tyrosine phosphorylation of Abp1 and translocation of both Abp1 and dynamin 2 from the cytoplasm to plasma membrane, where they colocalized with the BCR and cortical F-actin. Mutations of the two tyrosine phosphorylation sites of Abp1 and depolymerization of the actin cytoskeleton interfered with BCR-induced Abp1 recruitment to the plasma membrane. The inhibitory effect of a dynamin proline-rich domain deletion mutant on the recruitment of Abp1 to the plasma membrane, coimmunoprecipitation of dynamin with Abp1, and coprecipitation of Abp1 with GST fusion of the dyanmin proline-rich domain demonstrate the interaction of Abp1 with dynamin 2. These results demonstrate that the BCR regulates the function of Abp1 by inducing Abp1 phosphorylation and actin cytoskeleton rearrangement, and that Abp1 facilitates BCR-mediated Ag processing by simultaneously interacting with dynamin and the actin cytoskeleton.

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“…Cyclaseassociated protein (CAP) also rapidly associates with SIinduced punctate actin foci. 29 In yeast (S. cerevisiae), CAP/ Srv2p localises to actin patches and is required for the formation of F-actin aggregates 57 and is found in the actin 'bodies' in stressed, quiescent yeast. 58 As CAP/ Srv2p binds to adenylate cyclase and facilitates initiation of cAMP signalling during PCD initiation in yeast, 59 it may mediate foci formation and may, perhaps, link actin reorganisation to PCDsignalling networks in plant cells too.…”

Section: How Is Regulation Of the Cytoskeleton To Mediate Pcd Achieved?mentioning

confidence: 99%

Organisation and regulation of the cytoskeleton in plant programmed cell death

2011

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Programmed cell death (PCD) involves precise integration of cellular responses to extracellular and intracellular signals during both stress and development. In recent years much progress in our understanding of the components involved in PCD in plants has been made. Signalling to PCD results in major reorganisation of cellular components. The plant cytoskeleton is known to play a major role in cellular organisation, and reorganization and alterations in its dynamics is a well known consequence of signalling. There are considerable data that the plant cytoskeleton is reorganised in response to PCD, with remodelling of both microtubules and microfilaments taking place. In the majority of cases, the microtubule network depolymerises, whereas remodelling of microfilaments can follow two scenarios, either being depolymerised and then forming stable foci, or forming distinct bundles and then depolymerising. Evidence is accumulating that demonstrate that these cytoskeletal alterations are not just a consequence of signals mediating PCD, but that they also may have an active role in the initiation and regulation of PCD. Here we review key data from higher plant model systems on the roles of the actin filaments and microtubules during PCD and discuss proteins potentially implicated in regulating these alterations.

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Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton.

Abstract: In a variety of organisms, a number of proteins associated with the cortical actin cytoskeleton contain SH3 domains, suggesting that these domains may provide the physical basis for functional interactions among structural and regulatory proteins in the actin cytoskeleton. We

Cited by 164 publications

References 78 publications

Drebrin-like protein DBN-1 is a sarcomere component that stabilizes actin filaments during muscle contraction

Drebrin-like protein DBN-1 is a sarcomere component that stabilizes actin filaments during muscle contraction

Actin-Binding Protein 1 Regulates B Cell Receptor-Mediated Antigen Processing and Presentation in Response to B Cell Receptor Activation

Organisation and regulation of the cytoskeleton in plant programmed cell death

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