Membrane fusion induced by the major lipid-binding domain of the cytoskeletal protein talin

Isenberg, G.; Doerhoefer, Sabine; Hoekstra, Dick; Goldmann, Wolfgang H.

doi:10.1016/s0006-291x(02)00714-3

Cited by 15 publications

(13 citation statements)

References 45 publications

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“…Jahn and Sudhof 46 point out that fusion of intracellular membranes requires SNAREs (soluble N ‐ethylmaleimide‐sensitive factor attachment protein receptors), GTPases (guanosine triphosphatases), and Sec I/Munc‐18 proteins (SM‐proteins). Of special interest is the role of talin in membrane fusion because it is a member of the 4.1 superfamily and the ezrin, radixin, moesin family, and some tyrosine phosphatases 47 …”

Section: The Role Of Membrane Fusion In Vesiculationmentioning

confidence: 99%

The how and why of exocytic vesicles

Greenwalt¹

2005

Transfusion

183

155

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The purpose of this review is to draw the attention of general readers to the importance of cellular exocytic vesiculation as a normal mechanism of development and subsequent adjustment to changing conditions, focusing on red cell (RBC) vesiculation. Recent studies have emphasized the possible role of these microparticles as diagnostic and investigative tools. RBCs lose membrane, both in vivo and during ex vivo storage, by the blebbing of microvesicles from the tips of echinocytic spicules. Microvesicles shed by RBCs in vivo are rapidly removed by the reticuloendothelial system. During storage, this loss of membrane contributes to the storage lesion and the accumulation of the microvesicles are believed to be thrombogenic and thus to be clinically important.

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Section: The Role Of Membrane Fusion In Vesiculationmentioning

confidence: 99%

The how and why of exocytic vesicles

Greenwalt¹

2005

Transfusion

183

155

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“…The globular talin head contains a FERM (four-point-one, ezrin, radixin, moesin) domain (residues 86-400) with binding sites for β-integrin cytodomains [6], and two signalling proteins, FAK (focal adhesion kinase) [7] and the type 1γ 661 isoform of PIPK (phosphatidylinositol-4-phosphate 5-kinase) [8,9], which regulate the dynamic properties of integrin-containing cell-extracellular matrix junctions or FAs (focal adhesions). The FERM domain also contains an actin-binding site [10], and there is an adjacent membrane insertion sequence [11] which may account for the ability of talin to create holes in liposomes [12,13]. The talin rod, which is responsible for dimer formation, contains a conserved C-terminal actin-binding site [14,15] homologous to that in Hip1R (Huntingtin-interacting protein 1-related) and yeast Sla2p [16], a second integrin-binding site [17,18], and several binding sites for the cytoskeletal protein vinculin [19,20], which itself has multiple binding partners, including F-actin [21].…”

Section: Introductionmentioning

confidence: 99%

Genetic, biochemical and structural approaches to talin function

Critchley

2005

Biochemical Society Transactions

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“…Binding assays of talin on lipid membranes later revealed that the protein interacts simultaneously via its 47 kDa polypeptide domain with lipid bilayers and via its 200 kDa domain with actin [79]. Moreover, talin was found to trigger vesicle membrane fusion, which could be monitored using cryoelectron microscopy [80]. Hence, talin is of major importance for understanding cytoskeletal assembly and membrane targeting.…”

Section: Reviewmentioning

confidence: 99%

Model systems for studying cell adhesion and biomimetic actin networks

Brüggemann¹,

Frohnmayer²,

Spatz³

2014

Beilstein J. Nanotechnol.

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SummaryMany cellular processes, such as migration, proliferation, wound healing and tumor progression are based on cell adhesion. Amongst different cell adhesion molecules, the integrin receptors play a very significant role. Over the past decades the function and signalling of various such integrins have been studied by incorporating the proteins into lipid membranes. These proteolipid structures lay the foundation for the development of artificial cells, which are able to adhere to substrates. To build biomimetic models for studying cell shape and spreading, actin networks can be incorporated into lipid vesicles, too. We here review the mechanisms of integrin-mediated cell adhesion and recent advances in the field of minimal cells towards synthetic adhesion. We focus on reconstituting integrins into lipid structures for mimicking cell adhesion and on the incorporation of actin networks and talin into model cells.

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Membrane fusion induced by the major lipid-binding domain of the cytoskeletal protein talin

Cited by 15 publications

References 45 publications

The how and why of exocytic vesicles

The how and why of exocytic vesicles

Genetic, biochemical and structural approaches to talin function

Model systems for studying cell adhesion and biomimetic actin networks

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