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Spectrin‐actin interaction is required for neurite extension in NB 2a/dl neuroblastoma cells
Author(s) -
Sihag R.K.,
Shea T.B.,
Wang F.S.
Publication year - 1996
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/(sici)1097-4547(19960601)44:5<430::aid-jnr3>3.0.co;2-g
Subject(s) - spectrin , filopodia , neurite , actin , microbiology and biotechnology , cytoskeleton , microinjection , biology , cell , biochemistry , in vitro
Spectrin is an actin‐binding membrane skeleton protein involved in the maintenance of cell shape and generation of distinct membrane protein domains. Actin binds to the N‐terminal domain of β‐spectrin. To examine the function of spectrin‐actin interaction in neurons, we sought to disrupt this interaction in differentiating NB 2a neuroblastoma cells by microinjecting an N‐terminal domain‐specific anti‐β‐spectrin antibody. We found that microinjection of the affinity‐purified N‐terminal domain‐specific anti‐β‐spectrin inhibited the extension of the neurites in NB 2a/dl cells. The microinjected cells remained flat, and put out many filopodia‐like processes; but these processes failed to extend when the cells were induced to differentiate in the presence of dbc AMP or in serum‐free medium. The N‐terminal domain‐specific anti‐β‐spectrin also inhibited the binding of spectrin to actin. By contrast, the microinjection of monospecific anti‐α‐spectrin G did not inhibit neurite extension. These results suggest that β‐spectrin‐actin interaction may be required for neurite extension, which is critical for development of polarity in nerve cells. © 1996 Wiley‐Liss, Inc.