Mammalian actin binding protein 1 is essential for endocytosis but not lamellipodia formation: functional analysis by RNA interference

Mise-Omata, Setsuko; Montagne, Benjamin; Deckert, Marcel; Wienands, Jürgen; Acuto, Oreste

doi:10.1016/s0006-291x(02)02972-8

Cited by 48 publications

(48 citation statements)

References 20 publications

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“…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). In this study, we showed that Abp1 was required for efficient BCR-mediated Ag internalization, further demonstrating an essential role for Abp1 in endocytosis.…”

Section: Discussionmentioning

confidence: 54%

“…In mammalian cells, Abp1 accumulates in lamellipodia in response to growth factors or the expression of dominant-active Rac1 (28) and is involved in transferrin (Tf) receptor endocytosis by a direct interaction with dynamin (33), a GTPase that drives the release of the nascent clathrin-coated vesicles (38). The role of Abp1 in Tf receptor internalization was further confirmed in Abp1-deficient embryonic fibroblasts (39) and in cells where Abp1 was knocked down by small interfering RNA (40). Recently established Abp1 knockout mice exhibited a moderate reduction in synaptic endocytosis and a dramatic defect in the reformation of fusion-competent vesicles in synapses of hippocampal neurons (39).…”

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confidence: 92%

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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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Section: Discussionmentioning

confidence: 54%

mentioning

confidence: 92%

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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“…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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“…We found that cortactin, the Arp2/3 complex and Abp1 are enriched in these structures (Figure 3 and unpublished data). Similar to Hip1R, cortactin, and Abp1 are actin-binding proteins implicated in both endocytic and actin functions, and they may function at the interface between the actin cytoskeleton and the endocytic machinery (Kessels et al, 2000(Kessels et al, , 2001McNiven et al, 2000;Cao et al, 2003;Mise-Omata et al, 2003). Cortactin and Abp1 both colocalize with the Arp2/3 complex in cells (Kessels et al, 2000;McNiven et al, 2000).…”

Section: Accumulation Of Cortical Actin Tails and Other Unusual Cortimentioning

confidence: 99%

RNAi-mediated Hip1R Silencing Results in Stable Association between the Endocytic Machinery and the Actin Assembly Machinery

Engqvist-Goldstein

Zhang

Carréno

et al. 2004

MBoC

144

157

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Actin filaments transiently associate with the endocytic machinery during clathrin-coated vesicle formation. Although several proteins that might mediate or regulate this association have been identified, in vivo demonstration of such an activity has not been achieved. Huntingtin interacting protein 1R (Hip1R) is a candidate cytoskeletal-endocytic linker or regulator because it binds to clathrin and actin. Here, Hip1R levels were lowered by RNA interference (RNAi). Surprisingly, rather than disrupting the transient association between endocytic and cytoskeletal proteins, clathrin-coated structures (CCSs) and their endocytic cargo became stably associated with dynamin, actin, the Arp2/3 complex, and its activator, cortactin. RNAi double-depletion experiments demonstrated that accumulation of the cortical actin-endocytic complexes depended on cortactin. Fluorescence recovery after photobleaching showed that dynamic actin filament assembly can occur at CCSs. Our results provide evidence that Hip1R helps to make the interaction between actin and the endocytic machinery functional and transient.

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Mammalian actin binding protein 1 is essential for endocytosis but not lamellipodia formation: functional analysis by RNA interference

Cited by 48 publications

References 20 publications

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

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

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

RNAi-mediated Hip1R Silencing Results in Stable Association between the Endocytic Machinery and the Actin Assembly Machinery

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