Calcium-dependent regulation of actin filament bundling by lipocortin-85.

Ikebuchi, N W; Waisman, David M.

doi:10.1016/s0021-9258(19)39780-7

Cited by 108 publications

(34 citation statements)

References 72 publications

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“…Formation of actin bundles was assessed by electron microscopy (Ikebuchi and Waisman, 1990). Before centrifugation, aliquots (5 µl) were spread on electron grids and negatively stained with 1% uranyl acetate, and aggregates were observed using a transmission electron microscope (7500; Hitachi).…”

Section: In Vitro F-actin Binding Experimentsmentioning

confidence: 99%

Annexin A2–dependent actin bundling promotes secretory granule docking to the plasma membrane and exocytosis

Gabel

Delavoie

Demais

et al. 2015

Journal of Cell Biology

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Section: In Vitro F-actin Binding Experimentsmentioning

confidence: 99%

Annexin A2–dependent actin bundling promotes secretory granule docking to the plasma membrane and exocytosis

Gabel

Delavoie

Demais

et al. 2015

Journal of Cell Biology

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“…However, annexin II appears to be a multifunctional protein involved in endocytosis (reviewed in [14]), exocytosis (reviewed in [18]), DNA binding [19,20] and even extracellular processes (reviewed in [21]). In addition, annexin II is able to bind and bundle actin filaments in itro [22,23]. Earlier studies by two different groups suggested that annexin II is associated with cytoplasmic RNA [24,25].…”

Section: Introductionmentioning

confidence: 99%

Annexin II is associated with mRNAs which may constitute a distinct subpopulation

Vedeler

Hollås

2000

Biochemical Journal

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Protein-mRNA interactions affect mRNA transport, anchorage, stability and translatability in the cytoplasm. During the purification of three subpopulations of polysomes, it was observed that a 36-kDa protein, identified as annexin II, is associated with only one specific population of polysomes, namely cytoskeleton-associated polysomes. This association appears to be calcium-dependent since it was sensitive to EGTA and could be reconstituted in vitro. UV irradiation resulted in partial, EGTA-resistant cross-linking of annexin II to the polysomes. Binding of (32)P-labelled total RNA to proteins isolated from the cytoskeleton-bound polysomes on a NorthWestern blot resulted in a radioactive band having the same mobility as annexin II and, most importantly, purified native annexin II immobilized on nitrocellulose specifically binds mRNA. The mRNA population isolated from cytoskeleton-bound polysomes binds to annexin II with the highest affinity as compared with those isolated from free or membrane-bound polysomes. Interestingly, the annexin II complex, isolated from porcine small intestinal microvilli was a far better substrate for mRNA binding than the complex derived from transformed Krebs II ascites cells. When cytoskeleton-associated polysomes were split into 60 S and 40 S ribosomal subunits, and a peak containing mRNA complexes, annexin II fractionated with the mRNAs. Finally, using affinity purification of mRNA on poly(A)(+)-coupled magnetic beads, annexin II was only detected in association with messenger ribonucleoproteins (mRNPs) present in the cytoskeletal fraction (non-polysomal mRNPs). These results, derived from both in vitro experiments and cell fractionation, suggest that annexin II binds directly to the RNA moiety of mRNP complexes containing a specific population of mRNAs.

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“…To clarify the molecular linkage from the actin filaments to the plasma membrane in the cleavage furrow, the first protein that should be identified is an actin-modulating protein. Many actin-modulating proteins reportedly show high affinity for the plasma membranes; for example, gelsolin (Janmey et al, 1987;Hartwig et al, 1989), lipocortin-85 (lkebuchi andWaisman, 1990), myosin-I (Adams and Pollard, 1989;Miyata et al, 1989;Mooseker et al, 1989), actin-binding protein (Fox, 1985;Ohta et al, 1991), spectrin (for review see Bennet, 1989), the myristoylated, alaninerich C kinase substrate (Hartwig et al, 1992), and ponticulin (Shariff and Luna, 1990). However, none of them are reportedly concentrated in the cleavage furrow during cytokinesis.…”

mentioning

confidence: 99%

Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons.

Yonemura

Nagafuchi

Sato

et al. 1993

The Journal of Cell Biology

147

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Abstract. In leukocytes such as thymocytes and basophilic leukemia cells, a glycosilated integral membrane protein called CIM3 (leukosialin or sialophorin), which is defective in patients with WiskottAldrich syndrome, was highly concentrated in the cleavage furrow during cytokinesis. Not only at the mitotic phase but also at interphase, CIM3 was precisely colocalized with ezrin-radixin-moesin family members (ERM), which were previously reported to play an important role in the plasma membrane-actin filament association in general. At the electron microscopic level, throughout the cell cycle, both CIM3 and ERM were tightly associated with microvilli, providing membrane attachment sites for actin filaments. We constructed a cDNA encoding a chimeric molecule consisting of the extracellular domain of mouse E-cadherin and the transmembrane/cytoplasmic domain of rat CD43, and introduced it into mouse L fibroblasts lacking both endogenous CD43 and E-cadherin. In dividing transfectants, the chimeric molecules were concentrated in the cleavage furrow together with ERM, and both proteins were precisely colocalized throughout the cell cycle. Furthermore, using this transfection system, we narrowed down the domain responsible for the CD43-concentration in the cleavage furrow. Based on these findings, we conclude that CD43 is concentrated in the cleavage furrow through the direct or indirect interaction of its cytoplasmic domain with ERM and actin filaments.

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Calcium-dependent regulation of actin filament bundling by lipocortin-85.

Cited by 108 publications

References 72 publications

Annexin A2–dependent actin bundling promotes secretory granule docking to the plasma membrane and exocytosis

Annexin A2–dependent actin bundling promotes secretory granule docking to the plasma membrane and exocytosis

Annexin II is associated with mRNAs which may constitute a distinct subpopulation

Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons.

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