Characterization of intestinal microvillar membrane disks: detergent-resistant membrane sheets enriched in associated brush border myosin I (110K-calmodulin).

Mooseker, Mark S.; Conzelman, Karen A.; Coleman, Thomas R.; Heuser, John E.; Sheetz, Michael P.

doi:10.1083/jcb.109.3.1153

Cited by 58 publications

(18 citation statements)

References 37 publications

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“…As predicted by the primary structure and as previously shown for membrane fraction derived from intestinal cells, the entire BBMI protein and the proteins truncated in the motor domain were detected in association with membrane fraction derived from hepatoma (37). It is likely that the absence of enrichment for BBMI or the truncated BBMI in the bona fide membrane fraction is due to a soluble pool that could account also for the cytoplasmic diffuse staining observed for these proteins by immunofluorescence.…”

Section: Discussionmentioning

confidence: 54%

Brush border myosin-I truncated in the motor domain impairs the distribution and the function of endocytic compartments in an hepatoma cell line.

Dürrbach

Collins

Matsudaira

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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Myosins I, a ubiquitous monomeric class of myosins that exhibits actin-based motor properties, are associated with plasma and/or vesicular membranes and have been suggested as players for trafficking events between cell surface and intracellular membranous structures. To investigate the function of myosins I, we have transfected a mouse hepatoma cell line (BWTG3) with cDNAs encoding the chicken brush border myosin-I (BBMI) and two variants truncated in the motor domain. One variant is deleted of the first 446 amino acids and thereby lacks the ATP binding site, whereas the other is deleted of the entire motor domain and lacks the ATP and actin binding sites. We have observed (i) that significant amounts of the truncated variants are recovered with membrane fractions after cell fractionation, (ii) that they codistribute with a compartment containing a2-macroglobulin internalized for 30 min as determined by fluorescent microscopy, (iii) that the production of BBMI-truncated variants impairs the distribution of the acidic compartment and ligands internalized for 30 min, and (iv) that the production of the truncated variant containing the actin binding site decreases the rate of a2-macroglobulin degradation whereas the production of the variant lacking the ATP binding site and the actin binding site increases the rate of a2-macroglobulin degradation. These observations indicate that the two truncated variants have a dominant negative effect on the distribution and the function of the endocytic compartments. We propose that an unidentified myosin-I might contribute to the distribution of endocytic compartments in a juxtanuclear position and/or to the regulation of the delivery of ligands to the degradative compartment in BWTG3 cells.

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Section: Discussionmentioning

confidence: 54%

Brush border myosin-I truncated in the motor domain impairs the distribution and the function of endocytic compartments in an hepatoma cell line.

Dürrbach

Collins

Matsudaira

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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“…Cytochalasin D, which causes disruption of the actin filament network in addition to inhibiting polymerization [Schliwa, 19821, rapidly [Vale et al, 19851, including those of mobile varicosities Edmonds and Koenig, 19871, are one-to-two orders magnitude faster than in vitro actin-based translocation rates [Mooseker et al, 1989;Collins et al, 19901. Thus, the rate of movement during retraction is also consistent with an actomyosin driven process.…”

Section: Discussionmentioning

confidence: 98%

Characterization of the retraction response of goldfish retinal ganglion cell axons induced by monoclonal antibody 8A2 in vitro

Finnegan

Lemmon

Koenig

1992

Cell Motil. Cytoskeleton

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Retraction similar to that occurring spontaneously in senescent axonal fields of goldfish regenerating ganglion cell axons is reliably induced by inonoclonal antibody (mAb) 8A2. The retraction response is characterized by transformation of the growth cone into a nodular motile mass, which undergoes retrograde translocation in conjunction with the contiguous column of axoplasm, generating evacuated distal strands. The growth cone-to-motile mass transformation involves a reorganization of F-actin. In addition, the reorganization of F-actin is a necessary antecedent for retrograde bulk translocation of axoplasm. Contractile tension contributes to compaction within the motile mass, while that within the column of distal axoplasm is oriented longitudinally and appears to contribute to bulk movement. As a derivative of the growth cone, the motile mass exhibits protrusive activities and a capacity to translocate independently when microtubules are partially disrupted. Apparent compressive forces cause buckling of microtubules in the adjacent segment which appear as elbow-like protrusions. Cytochalasin D blocks mAb 8A2 induced retraction and immediately arrests retrograde translocation when it is in progress; however, neither nocodazole nor taxol blocks retraction. Phalloidin and immunofluorescence double labeling of retracted axons reveals that myosin 11, MLCK, and calmodulin co-localize with dense F-actin structures within the motile mass. These results suggest that microtubules play a subordinate, passive role, and that actomyosin interactions mediate the formation of the motile mass and the retraction response. Finally, axons grown on laminin exhibit a more robust retraction response than those grown on polylysine, implicating membrane-cytoskeletal interactions as modulating factors. 0 1992 W i l e y -I k , Inc.

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“…myosin 2) to dimerize. Like other myosins, BBM1 has actin-stimulated ATPase activity and, in the presence of ATP and calcium, generates movement along actin filaments (7,8). BBM1 is capable of binding both to the actin core and to the membrane of the microvillus (7, 9 -11).…”

mentioning

confidence: 99%

“…BBM1 is capable of binding both to the actin core and to the membrane of the microvillus (7, 9 -11). Binding to the membrane alters its activity by as yet uncertain mechanisms (7,12). Binding to the membrane appears to involve the C-terminal portion of the molecule and requires acidic phospholipids (13).…”

mentioning

confidence: 99%

Zipper Protein, a B-G Protein with the Ability to Regulate Actin/Myosin 1 Interactions in the Intestinal Brush Border

Bikle

Munson

Kömüves

1996

Journal of Biological Chemistry

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We recently identified a 28-kDa protein in the intestinal brush border that resembled tropomyosin in terms of size, homology, and ␣ helical content. This protein contained 27 heptad repeats, nearly all of which began with leucine, leading to its name zipper protein. Subsequent analysis, however, indicated that both a 49-kDa and a 28-kDa immunoreactive protein existed in intestinal brush-border extracts. Using 5-rapid amplification of cDNA ends analysis, we extended the N-terminal sequence of zipper protein to the apparent translation start site. This additional sequence contained a putative transmembrane domain and two potential tryptic cleavage sites C-terminal to the transmembrane domain which would release a 28-kDa cytoplasmic protein if utilized. The additional sequence was highly homologous to members of the B-G protein family, a family with no known function. Immunoelectron microscopy showed that zipper protein was confined to the membrane of the microvillus where it was in close association with brush-border myosin 1 (BBM1). Recombinant zipper protein (28-kDa cytoplasmic portion) blocked the binding of actin to BBM1 and inhibited actin-stimulated BBM1 ATPase activity. In contrast, zipper protein had no effect on endogenous or K/EDTA-stimulated BBM1 ATPase activity. Furthermore, zipper protein displaced tropomyosin from binding to actin, suggesting that these homologous proteins bind to the same sites on the actin molecule. We conclude that zipper protein is a transmembrane protein of the B-G family localized to the intestinal epithelial cell microvillus. The extended cytoplasmic tail either in the intact molecule or after tryptic cleavage may participate in regulating the binding and, thus, activation of BBM1 by actin in a manner similar to tropomyosin.

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Characterization of intestinal microvillar membrane disks: detergent-resistant membrane sheets enriched in associated brush border myosin I (110K-calmodulin).

Cited by 58 publications

References 37 publications

Brush border myosin-I truncated in the motor domain impairs the distribution and the function of endocytic compartments in an hepatoma cell line.

Brush border myosin-I truncated in the motor domain impairs the distribution and the function of endocytic compartments in an hepatoma cell line.

Characterization of the retraction response of goldfish retinal ganglion cell axons induced by monoclonal antibody 8A2 in vitro

Zipper Protein, a B-G Protein with the Ability to Regulate Actin/Myosin 1 Interactions in the Intestinal Brush Border

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