Biochemical and immunochemical analysis of rat brain dynamin interaction with microtubules and organelles in vivo and in vitro.

Scaife, Rob; Margolis, Robert L.

doi:10.1083/jcb.111.6.3023

Cited by 106 publications

(79 citation statements)

References 41 publications

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“…Since dynamin is substantially a neuronal protein (Scaife and Margolis, 1990;Nakata et al, 1993), it might be argued that such dynamin dependent coupling processes might occur only in neurons. Recently, however, a dynamin homolog, dynamin 2, has been discovered (Cook et al, 1994) which has widespread tissue distribution, so it is now possible to imagine similar functions occurring in a variety of tissues.…”

Section: Discussionmentioning

confidence: 99%

Growth factor-induced binding of dynamin to signal transduction proteins involves sorting to distinct and separate proline-rich dynamin sequences.

et al. 1994

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Dynamin, a 100 kDa GTPase, is critical for endocytosis, synaptic transmission and neurogenesis. Endocytosis accompanies receptor processing and plays an essential role in attenuating receptor tyrosine kinase signal transduction. Dynamin has been demonstrated to be involved in the endocytic processing at the cell surface and may play a general role in coupling receptor activation to endocytosis. Src homology (SH) domain dependent protein‐protein interactions are important to tyrosine kinase receptor signal transduction. The C‐terminus of dynamin contains two clusters of SH3 domain binding proline motifs; these motifs may interact with known SH3 domain proteins during tyrosine kinase receptor activation. We demonstrate here that SH3 domain‐containing signal transduction proteins, such as phospholipase C gamma‐1 (PLC gamma‐1), do indeed bind to dynamin in a growth factor inducible manner. The induction of PLC gamma‐1 binding to dynamin occurs within minutes of the addition of platelet derived growth factor (PDGF) to cells. Binding of these signal transduction proteins to dynamin involves specific sorting to individual proline motif clusters and appears to be responsible for co‐immunoprecipitation of tyrosine phosphorylated PDGF receptors with dynamin following PDGF stimulation of mammalian cells. The binding of dynamin to SH3 domain‐containing proteins may therefore be important for formation of the protein complex required for the endocytic processing of activated tyrosine kinase receptors.

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Section: Discussionmentioning

confidence: 99%

Growth factor-induced binding of dynamin to signal transduction proteins involves sorting to distinct and separate proline-rich dynamin sequences.

et al. 1994

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“…Three mammalian dynamin isoforms are known (1,3,9). DynaminϪ1 is expressed only in neurons (10,11), dynaminϪ2 is ubiquitously expressed (11,12), while dynaminϪ3 is restricted primarily to the testes (13). Each isoform has multiple domains.…”

mentioning

confidence: 99%

The Pleckstrin Homology Domains of Dynamin Isoforms Require Oligomerization for High Affinity Phosphoinositide Binding

Klein

Lee

Frank³

et al. 1998

Journal of Biological Chemistry

194

181

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The dynamins are 100-kDa GTPases involved in the scission event required for formation of endocytotic vesicles. The two main described mammalian dynamins (dynamin؊1 and dynamin؊2) both contain a pleckstrin homology (PH) domain, which has been implicated in dynamin binding to (and activation by) acidic phospholipids, most notably phosphoinositides. We demonstrate that the PH domains of both dynamin isoforms require oligomerization for high affinity phosphoinositide binding. Strong phosphoinositide binding was detected only when the PH domains were dimerized by fusion to glutathione S-transferase, or via a single engineered intermolecular disulfide bond. Phosphoinositide binding specificities agreed reasonably with reported effects of different phospholipids on dynamin GTPase activity. Although they differ in their ability to inhibit rapid endocytosis in adrenal chromaffin cells, the dynamin؊1 and dynamin؊2 PH domains showed identical phosphoinositide binding specificities. Since oligomerization is required for binding of the dynamin PH domain to phosphoinositides, it follows that PH domain-mediated phosphoinositide binding will favor oligomerization of intact dynamin (which has an inherent tendency to self-associate). We propose that the dynamin PH domain thus mediates the observed cooperative binding of dynamin to membranes containing acidic phospholipids and promotes the self-assembly that is critical for both stimulation of its GTPase activity and its ability to achieve membrane scission.

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“…The mammalian brain dynamin was exclusively expressed in neurons (Scaife & Margolis, 1990), preferentially after postnatal day 7 (Nakata et al, 1991). This neuron-specific isoform is termed dynamin 1 after two other isoforms with different tissue distributions were identified.…”

Section: Dynamin Isoforms and Their Expressionmentioning

confidence: 99%

Etiological Role of Dynamin in Charcot-Marie-Tooth Disease

Takei¹,

Tanabe²

2012

Peripheral Neuropathy - Advances in Diagnostic and Therapeutic Approaches

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Biochemical and immunochemical analysis of rat brain dynamin interaction with microtubules and organelles in vivo and in vitro.

Cited by 106 publications

References 41 publications

Growth factor-induced binding of dynamin to signal transduction proteins involves sorting to distinct and separate proline-rich dynamin sequences.

Growth factor-induced binding of dynamin to signal transduction proteins involves sorting to distinct and separate proline-rich dynamin sequences.

The Pleckstrin Homology Domains of Dynamin Isoforms Require Oligomerization for High Affinity Phosphoinositide Binding

Etiological Role of Dynamin in Charcot-Marie-Tooth Disease

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