NDLI: Nonneuronal isoforms of STOP protein are responsible for microtubule cold stability in mammalian fibroblasts

Content Provider	PubMed Central
Author	Eric, Denarier Anne, Fourest-lieuvin Bosc, Christophe Pirollet, Fabienne Chapel, Agnès Margolis, Robert L. Job, Didier
Copyright Year	1998
Abstract	A number of cycling mammalian cells, such as NIH 3T3, contain abundant subsets of cold-stable microtubules. The origin of such microtubule stabilization in nonneuronal cells is unknown. We have previously described a neuronal protein, stable tubule-only polypeptide (STOP), that binds to microtubules and induces cold stability. We find that NIH 3T3 fibroblasts contain a major 42-kDa isoform of STOP (fibroblastic STOP, F-STOP). F-STOP contains the central repeats characteristic of brain STOP but shows extensive deletions of N- and C-terminal protein domains that are present in brain STOP. These deletions arise from differences in STOP RNA splicing. Despite such deletions, F-STOP has full microtubule stabilizing activity. F-STOP accumulates on cold-stable microtubules of interphase arrays and is present on stable microtubules within the mitotic spindle of NIH 3T3 cells. STOP inhibition by microinjection of affinity-purified STOP central repeat antibodies into NIH 3T3 cells abolishes both interphase and spindle microtubule cold stability. Similar results were obtained with Rat2 cells. These results show that STOP proteins have nonneuronal isoforms that are responsible for the microtubule cold stability observed in mammalian fibroblasts.
Starting Page	6055
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	11
Volume Number	95
Language	English
Publisher	The National Academy of Sciences
Publisher Date	1998-05-26
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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STOP Proteins are Responsible for the High Degree of Microtubule Stabilization Observed in Neuronal Cells

STOP proteins are responsible for the high degree of microtubule stabilization observed in neuronal cells (1998)

Cloning, expression, and properties of the microtubule-stabilizing protein STOP.

Bmcc1s, a novel brain-isoform of bmcc1, affects cell morphology by regulating map6/stop functions.

Regulation of microtubule cold stability by calmodulin-dependent and -independent phosphorylation.

STOP Proteins are Responsible for the High Degree of Microtubule Stabilization Observed in Neuronal Cells

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The fragile X protein controls microtubule-associated protein 1B translation and microtubule stability in brain neuron development

Low molecular weight microtubule-associated proteins are light chains of microtubule-associated protein 1 (MAP 1).

Nonneuronal isoforms of STOP protein are responsible for microtubule cold stability in mammalian fibroblasts

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STOP Proteins are Responsible for the High Degree of Microtubule Stabilization Observed in Neuronal Cells

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Cloning, expression, and properties of the microtubule-stabilizing protein STOP.

Bmcc1s, a novel brain-isoform of bmcc1, affects cell morphology by regulating map6/stop functions.

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