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{{Short description|Vesicle formation GTPase family}}
{{Infobox protein family
{{Infobox protein family
| Symbol = Dynamin_N
| Symbol = Dynamin_N
| Name = Dynamin_N
| Name = Dynamin family
| image = PDB 2aka EBI.jpg
| image = PDB 2aka EBI.jpg
| width =
| width =
| caption = structure of the nucleotide-free myosin ii motor domain from dictyostelium discoideum fused to the gtpase domain of dynamin 1 from rattus norvegicus
| caption = Structure of the nucleotide-free myosin II motor domain from ''Dictyostelium discoideum'' fused to the GTPase domain of dynamin I from ''Rattus norvegicus''
| Pfam = PF00350
| Pfam = PF00350
| Pfam_clan = CL0023
| Pfam_clan = CL0023
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| image = PDB 2aka EBI.jpg
| image = PDB 2aka EBI.jpg
| width =
| width =
| caption = structure of the nucleotide-free myosin ii motor domain from dictyostelium discoideum fused to the gtpase domain of dynamin 1 from rattus norvegicus
| caption = Structure of the nucleotide-free myosin II motor domain from ''Dictyostelium discoideum'' fused to the GTPase domain of dynamin I from ''Rattus norvegicus''
| Pfam = PF01031
| Pfam = PF01031
| Pfam_clan =
| Pfam_clan =
Line 37: Line 38:
| CDD =
| CDD =
}}
}}
'''Dynamin''' is a [[GTPase]] responsible for [[endocytosis]] in the eukaryotic cell. Dynamins are principally involved in the scission of newly formed [[vesicle (biology)|vesicles]] from the membrane of one cellular compartment and their targeting to, and fusion with, another compartment, both at the cell surface (particularly [[caveolae]] internalization) as well as at the [[Golgi apparatus]].<ref name= Henley>Henley, J.R., Cao, H., McNicven, M.A. (1999). [http://www.fasebj.org/cgi/content/full/13/9002/S243 “Participation of dynamin in the biogenesis of cytoplasmic vesicles”.] ''The FASEB Journal'', 13, S243-S247.</ref><ref name= Hinshaw>Hinshaw, J. [http://dynamin.niddk.nih.gov/ “Dynamin overview: The Role of Dynamin in Membrane Fission”.] National institute of diabetes & digestive & kidney diseases, Laboratory of cell biochemistry and biology. accessed 021806.</ref><ref name= Urrutia>{{cite journal | doi = 10.1073/pnas.94.2.377 | last1 = Urrutia | first1 = R. | last2 = Henley | first2 = J.R. | last3 = Cook | first3 = T. | last4 = McNiven | first4 = M.A. | year = 1997 | title = The dynamins: Redundant or distinct functions for an expanding family of related GTPases? | url = http://www.pnas.org/cgi/content/full/94/2/377?ijkey=cc76b66f40ce6a1c4bef3246109754c5ca3cc425 | journal = [[Proc. Natl Acad. Sci. USA]] | volume = 94 | issue = 2| pages = 377–384 }}</ref> Dynamin also plays a role in many processes including division of [[organelle]]s,<ref name="pmid16218949">{{cite journal | author = Thoms S, Erdmann R | title = Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation. | journal = FEBS J | volume = 272 | issue = 20 | pages = 5169–81 | year = 2005 | month = Oct | pmid = 16218949 | pmc = | doi =10.1111/j.1742-4658.2005.04939.x }}</ref> [[cytokinesis]] and microbial [[pathogen]] resistance.
'''Dynamin''' is a [[GTPase]] responsible for [[endocytosis]] in the eukaryotic cell. Dynamin is part of the "[[dynamin superfamily]]", which includes classical dynamins, dynamin-like proteins, [[MX1|Mx proteins]], [[OPA1]], [[MFN1|mitofusins]], and [[Guanylate-binding protein|GBP]]s. Members of the dynamin family are principally involved in the scission of newly formed [[vesicle (biology)|vesicles]] from the membrane of one cellular compartment and their targeting to, and fusion with, another compartment, both at the cell surface (particularly [[caveolae]] internalization) as well as at the [[Golgi apparatus]].<ref name= Henley>{{Cite journal|title=Participation of dynamin in the biogenesis of cytoplasmic vesicles|first1=John R.|last1=Henley|first2=Hong|last2=Cao|first3=Mark A.|last3=McNiven|date=December 16, 1999|journal=The FASEB Journal|volume=13|issue=9002|pages=S243-7 |doi=10.1096/fasebj.13.9002.S243|doi-access=free |pmid=10619136 |s2cid=24401725 }}</ref><ref name= Hinshaw>Hinshaw, J. [http://www2.niddk.nih.gov/NIDDKLabs/IntramuralFaculty/HinshawJenny.htm "Research statement, Jenny E. Hinshaw, Ph.D."] {{Webarchive|url=https://web.archive.org/web/20210715052253/https://www.niddk.nih.gov/NIDDKLabs/IntramuralFaculty/HinshawJenny.htm |date=2021-07-15 }} National Institute of Diabetes & Digestive & Kidney Diseases, Laboratory of Cell Biochemistry and Biology. Accessed 19 March 2013.</ref><ref name= Urrutia>{{cite journal | vauthors = Urrutia R, Henley JR, Cook T, McNiven MA | title = The dynamins: redundant or distinct functions for an expanding family of related GTPases? | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 94 | issue = 2 | pages = 377–384 | date = January 1997 | pmid = 9012790 | pmc = 34135 | doi = 10.1073/pnas.94.2.377 | bibcode = 1997PNAS...94..377U | doi-access = free }}</ref> Dynamin family members also play a role in many processes including division of [[organelle]]s,<ref name="pmid16218949">{{cite journal | vauthors = Thoms S, Erdmann R | title = Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation | journal = The FEBS Journal | volume = 272 | issue = 20 | pages = 5169–5181 | date = October 2005 | pmid = 16218949 | doi = 10.1111/j.1742-4658.2005.04939.x | doi-access = }}</ref> [[cytokinesis]] and microbial [[pathogen]] resistance.


== Structure ==
Dynamin is part of the "Dynamin Superfamily," which includes classical dynamins, dynamin-like proteins, Mx proteins, OPA, mitofusins, and GBPs. Dynamin itself is a 96 [[kilodalton|kDa]] [[enzyme]], and was first isolated when researchers were attempting to isolate new [[microtubule]]-based motors from the bovine brain. Dynamin has been extensively studied within [[clathrin]]-coated vesicle budding from the [[cell membrane]].<ref name= Urrutia/><ref name= McMahon>McMahon. (2004). [http://www.endocytosis.org/Dynamin/index.html “Researching Endocytic Mechanisms: Dynamin:.] Accompaniment of Nature Reviews on Molecular Cell Biology, 5, 133-147.</ref>
[[File:Dynamin assembles into spirals.jpg|thumb|left|Dynamin assembled into helical polymers as visualized by negative stain electron microscopy.<ref>{{cite journal | vauthors = Hinshaw JE, Schmid SL | title = Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding | journal = Nature | volume = 374 | issue = 6518 | pages = 190–192 | date = March 1995 | pmid = 7877694 | doi = 10.1038/374190a0 | bibcode = 1995Natur.374..190H | s2cid = 4365628 }}</ref>|alt=]]

Dynamin itself is a 96 [[kilodalton|kDa]] [[enzyme]], and was first isolated when researchers were attempting to isolate new [[microtubule]]-based motors from the bovine brain. Dynamin has been extensively studied in the context of [[clathrin]]-coated vesicle budding from the [[cell membrane]].<ref name= Urrutia/><ref name= McMahon>{{cite journal | vauthors = Praefcke GJ, McMahon HT | title = The dynamin superfamily: universal membrane tubulation and fission molecules? | journal = Nature Reviews. Molecular Cell Biology | volume = 5 | issue = 2 | pages = 133–147 | date = February 2004 | pmid = 15040446 | doi = 10.1038/nrm1313 | s2cid = 6305282 }}</ref> Beginning from the [[N-terminus]], Dynamin consists of a GTPase domain connected to a helical stalk domain via a flexible neck region containing a Bundle Signalling Element and [https://www.ebi.ac.uk/interpro/entry/IPR020850 GTPase Effector Domain]. At the opposite end of the stalk domain is a loop that links to a membrane-binding [[Pleckstrin homology domain]]. The protein strand then loops back towards the GTPase domain and terminates with a [[Proline rich protein|Proline Rich Domain]] that binds to the [[Src homology domain|Src Homology domains]] of many proteins.


== Function ==
== Function ==
As a vesicle invaginates, dynamin forms a spiral around the neck of the vesicle. Once the spiral is in place, it extends lengthwise and constricts through [[GTPase#Mechanism|GTP hydrolysis]]. This lengthening and tightening of the coil around the vesicle neck causes it to break and results in the pinching off of the vesicle from the parent membrane. An example of a vesicle is a clathrin-coated pit.<ref name= Hinshaw/><ref name= McMahon/>


During clathrin-mediated endocytosis, the cell membrane invaginates to form a budding vesicle. Dynamin binds to and assembles around the neck of the endocytic vesicle, forming a helical polymer arranged such that the GTPase domains dimerize in an asymmetric manner across helical rungs.<ref>{{cite journal | vauthors = Sundborger AC, Fang S, Heymann JA, Ray P, Chappie JS, Hinshaw JE | title = A dynamin mutant defines a superconstricted prefission state | journal = Cell Reports | volume = 8 | issue = 3 | pages = 734–742 | date = August 2014 | pmid = 25088425 | pmc = 4142656 | doi = 10.1016/j.celrep.2014.06.054 }}</ref><ref name=":0" /> The polymer constricts the underlying membrane upon [[GTPase#Mechanism|GTP binding and hydrolysis]] via conformational changes emanating from the flexible neck region that alters the overall helical symmetry.<ref name=":0">{{cite journal | vauthors = Kong L, Sochacki KA, Wang H, Fang S, Canagarajah B, Kehr AD, Rice WJ, Strub MP, Taraska JW, Hinshaw JE | display-authors = 6 | title = Cryo-EM of the dynamin polymer assembled on lipid membrane | journal = Nature | volume = 560 | issue = 7717 | pages = 258–262 | date = August 2018 | pmid = 30069048 | pmc = 6121775 | doi = 10.1038/s41586-018-0378-6 | bibcode = 2018Natur.560..258K }}</ref> Constriction around the vesicle neck leads to the formation of a hemi-fission membrane state that ultimately results in membrane scission.<ref name= Hinshaw/><ref name= McMahon/><ref>{{cite journal | vauthors = Mattila JP, Shnyrova AV, Sundborger AC, Hortelano ER, Fuhrmans M, Neumann S, Müller M, Hinshaw JE, Schmid SL, Frolov VA | display-authors = 6 | title = A hemi-fission intermediate links two mechanistically distinct stages of membrane fission | journal = Nature | volume = 524 | issue = 7563 | pages = 109–113 | date = August 2015 | pmid = 26123023 | pmc = 4529379 | doi = 10.1038/nature14509 | bibcode = 2015Natur.524..109M }}</ref> Constriction may be in part the result of the twisting activity of dynamin, which makes dynamin the only [[molecular motor]] known to have a twisting activity.<ref name= Roux>{{cite journal | vauthors = Roux A, Uyhazi K, Frost A, De Camilli P | title = GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission | journal = Nature | volume = 441 | issue = 7092 | pages = 528–531 | date = May 2006 | pmid = 16648839 | doi = 10.1038/nature04718 | bibcode = 2006Natur.441..528R | s2cid = 4413887 }}</ref>
To view the effect of GTP and GDP on dynamin spirals, follow this link: http://dynamin.niddk.nih.gov/figure2.html.<ref name= Hinshaw/> In part A of this picture we see dynamin tubes in the absence of GTP; they are large and relaxed. In part B of the picture we see the same dynamin tubes from part one but after addition of GTP, GTP is hydrolysed because of intrinsic GTPase activity and constriction ensues. This is how dynamin works to pinch vesicles off from the membrane.

To view a ‘cartoon’ image of the non-constricted and constricted state of dynamin spirals, please follow this link: http://dynamin.niddk.nih.gov/figure5.html.<ref name= Hinshaw/> The first structure on the left is dynamin in its relaxed state. The structure on the right is dynamin in its constricted state. This allows you to see how much dynamin tightens and changes when GTP is converted to GDP.<ref name= Henley/>

This constriction is in part the result of the twisting activity of dynamin <ref name= Roux>{{cite journal | last1 = Roux | first1 = A | last2 = Uyhazi | first2 = K | last3 = Frost | first3 = A | last4 = De Camilli | first4 = P | title = GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission | url = http://www.nature.com/nature/journal/v441/n7092/abs/nature04718.html;jsessionid=B2DCD26EE59C1918B5A66ECA9542A843 | journal = Nature a - z index | volume = 441 | issue = 7092 | pages = 528–31 | date = 2006-04-30 | pmid = 16648839 | doi = 10.1038/nature04718 }}</ref> This twisting is strictly dependent on its GTPase activity. Dynamin is the only [[molecular motor]] known to have a twisting activity. Dynamin is a right-handed helix, and has a right-handed twisting activity that explains its tightening and the pitch reduction described above.


==Types==
==Types==
In mammals, three different dynamin genes have been identified.
In mammals, three different dynamin genes have been identified with key sequence differences in their Pleckstrin homology domains leading to differences in the recognition of lipid membranes:


⚫
* [[DNM2|Dynamin II]] is expressed in most cell types;
* [[DNM1|Dynamin I]] is expressed in [[neuron]]s and [[neuroendocrine cell]]s
* [[DNM1|Dynamin I]] is expressed in [[neuron]]s and [[neuroendocrine cell]]s
⚫
* [[DNM2|Dynamin II]] is expressed in most cell types
* [[DNM3|Dynamin III]] is strongly expressed in the [[testis]], but is also present in [[heart]], [[brain]], and [[lung]] tissue.<ref name= Henley/><ref name= McMahon/>
* [[DNM3|Dynamin III]] is strongly expressed in the [[testis]], but is also present in [[heart]], [[brain]], and [[lung]] tissue.<ref name= Henley/><ref name= McMahon/>


== Pharmacology ==
⚫
==Disease implications==
Small molecule inhibitors of dynamin activity have been developed, including Dynasore<ref>{{cite journal | vauthors = Macia E, Ehrlich M, Massol R, Boucrot E, Brunner C, Kirchhausen T | title = Dynasore, a cell-permeable inhibitor of dynamin | language = English | journal = Developmental Cell | volume = 10 | issue = 6 | pages = 839–850 | date = June 2006 | pmid = 16740485 | doi = 10.1016/j.devcel.2006.04.002 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Eschenburg S, Reubold TF | title = Modulation of dynamin function by small molecules | journal = Biological Chemistry | volume = 399 | issue = 12 | pages = 1421–1432 | date = November 2018 | pmid = 30067507 | doi = 10.1515/hsz-2018-0257 | s2cid = 51895475 | doi-access = free }}</ref> and photoswitchable derivatives (Dynazo)<ref>{{cite journal | vauthors = Camarero N, Trapero A, Pérez-Jiménez A, Macia E, Gomila-Juaneda A, Martín-Quirós A, Nevola L, Llobet A, Llebaria A, Hernando J, Giralt E, Gorostiza P | display-authors = 6 | title = Correction: Photoswitchable dynasore analogs to control endocytosis with light | journal = Chemical Science | volume = 11 | issue = 35 | pages = 9712 | date = September 2020 | pmid = 33016959 | pmc = 7495901 | doi = 10.1039/D0SC90189J }}</ref> for spatiotemporal control of endocytosis with light ([[photopharmacology]]).
Mutations in [[DNM2|Dynamin II]] have been found to cause dominant intermediate [[Charcot-Marie-Tooth disease]].<ref>{{Cite journal
| author = [[Stephan Zuchner]], [[Maher Noureddine]], [[Marina Kennerson]], [[Kristien Verhoeven]], [[Kristl Claeys]], [[Peter De Jonghe]], [[John Merory]], [[Sofia A. Oliveira]], [[Marcy C. Speer]], [[Judith E. Stenger]], [[Gina Walizada]], [[Danqing Zhu]], [[Margaret A. Pericak-Vance]], [[Garth Nicholson]], [[Vincent Timmerman]] & [[Jeffery M. Vance]]
| title = Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease
| journal = [[Nature genetics]]
| volume = 37
| issue = 3
| pages = 289–294
| year = 2005
| month = March
| doi = 10.1038/ng1514
| pmid = 15731758
}}</ref>


⚫
== Disease implications ==
==References==
Mutations in [[DNM2|Dynamin II]] have been found to cause dominant intermediate [[Charcot-Marie-Tooth disease]].<ref>{{cite journal | vauthors = Züchner S, Noureddine M, Kennerson M, Verhoeven K, Claeys K, De Jonghe P, Merory J, Oliveira SA, Speer MC, Stenger JE, Walizada G, Zhu D, Pericak-Vance MA, Nicholson G, Timmerman V, Vance JM | display-authors = 6 | title = Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease | journal = Nature Genetics | volume = 37 | issue = 3 | pages = 289–294 | date = March 2005 | pmid = 15731758 | doi = 10.1038/ng1514 | s2cid = 19191581 }}</ref>
⚫
{{reflist|2}}
Epileptic encephalopathy–causing de novo mutations in dynamin have been suggested to cause dysfunction of vesicle scission during synaptic vesicle endocytosis.<ref name="Dhindsa">{{cite journal | vauthors = Dhindsa RS, Bradrick SS, Yao X, Heinzen EL, Petrovski S, Krueger BJ, Johnson MR, Frankel WN, Petrou S, Boumil RM, Goldstein DB | display-authors = 6 | title = Epileptic encephalopathy-causing mutations in DNM1 impair synaptic vesicle endocytosis | journal = Neurology. Genetics | volume = 1 | issue = 1 | pages = e4 | date = June 2015 | pmid = 27066543 | pmc = 4821085 | doi = 10.1212/01.NXG.0000464295.65736.da }}</ref>


==External links==
== References ==
⚫
{{reflist}}

== External links ==
{{Commons category|Dynamins}}
* {{MeshName|Dynamins}}
* {{MeshName|Dynamins}}


{{Vesicular transport proteins}}
{{Vesicular transport proteins}}
{{GTPases}}
{{Cytoskeletal Proteins}}
{{Cytoskeletal Proteins}}
{{Acid anhydride hydrolases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}


[[Category:Cellular processes]]
[[Category:Cellular processes]]
[[Category:EC 3.6.5]]
[[Category:EC 3.6.5]]

[[ca:Dinamina]]
[[cs:Dynamin]]
[[de:Dynamine]]
[[es:Dinamina]]
[[fr:Dynamine]]
[[pt:Dinamina]]
[[ru:Динамин]]

Latest revision as of 09:31, 5 June 2024

Dynamin family
Structure of the nucleotide-free myosin II motor domain from Dictyostelium discoideum fused to the GTPase domain of dynamin I from Rattus norvegicus
Identifiers
SymbolDynamin_N
PfamPF00350
Pfam clanCL0023
InterProIPR001401
PROSITEPDOC00362
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Dynamin central region
Structure of the nucleotide-free myosin II motor domain from Dictyostelium discoideum fused to the GTPase domain of dynamin I from Rattus norvegicus
Identifiers
SymbolDynamin_M
PfamPF01031
InterProIPR000375
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Dynamin is a GTPase responsible for endocytosis in the eukaryotic cell. Dynamin is part of the "dynamin superfamily", which includes classical dynamins, dynamin-like proteins, Mx proteins, OPA1, mitofusins, and GBPs. Members of the dynamin family are principally involved in the scission of newly formed vesicles from the membrane of one cellular compartment and their targeting to, and fusion with, another compartment, both at the cell surface (particularly caveolae internalization) as well as at the Golgi apparatus.[1][2][3] Dynamin family members also play a role in many processes including division of organelles,[4] cytokinesis and microbial pathogen resistance.

Structure

[edit]
Dynamin assembled into helical polymers as visualized by negative stain electron microscopy.[5]

Dynamin itself is a 96 kDa enzyme, and was first isolated when researchers were attempting to isolate new microtubule-based motors from the bovine brain. Dynamin has been extensively studied in the context of clathrin-coated vesicle budding from the cell membrane.[3][6] Beginning from the N-terminus, Dynamin consists of a GTPase domain connected to a helical stalk domain via a flexible neck region containing a Bundle Signalling Element and GTPase Effector Domain. At the opposite end of the stalk domain is a loop that links to a membrane-binding Pleckstrin homology domain. The protein strand then loops back towards the GTPase domain and terminates with a Proline Rich Domain that binds to the Src Homology domains of many proteins.

Function

[edit]

During clathrin-mediated endocytosis, the cell membrane invaginates to form a budding vesicle. Dynamin binds to and assembles around the neck of the endocytic vesicle, forming a helical polymer arranged such that the GTPase domains dimerize in an asymmetric manner across helical rungs.[7][8] The polymer constricts the underlying membrane upon GTP binding and hydrolysis via conformational changes emanating from the flexible neck region that alters the overall helical symmetry.[8] Constriction around the vesicle neck leads to the formation of a hemi-fission membrane state that ultimately results in membrane scission.[2][6][9] Constriction may be in part the result of the twisting activity of dynamin, which makes dynamin the only molecular motor known to have a twisting activity.[10]

Types

[edit]

In mammals, three different dynamin genes have been identified with key sequence differences in their Pleckstrin homology domains leading to differences in the recognition of lipid membranes:

Pharmacology

[edit]

Small molecule inhibitors of dynamin activity have been developed, including Dynasore[11][12] and photoswitchable derivatives (Dynazo)[13] for spatiotemporal control of endocytosis with light (photopharmacology).

Disease implications

[edit]

Mutations in Dynamin II have been found to cause dominant intermediate Charcot-Marie-Tooth disease.[14] Epileptic encephalopathy–causing de novo mutations in dynamin have been suggested to cause dysfunction of vesicle scission during synaptic vesicle endocytosis.[15]

References

[edit]
  1. ^ a b Henley, John R.; Cao, Hong; McNiven, Mark A. (December 16, 1999). "Participation of dynamin in the biogenesis of cytoplasmic vesicles". The FASEB Journal. 13 (9002): S243-7. doi:10.1096/fasebj.13.9002.S243. PMID 10619136. S2CID 24401725.
  2. ^ a b Hinshaw, J. "Research statement, Jenny E. Hinshaw, Ph.D." Archived 2021-07-15 at the Wayback Machine National Institute of Diabetes & Digestive & Kidney Diseases, Laboratory of Cell Biochemistry and Biology. Accessed 19 March 2013.
  3. ^ a b Urrutia R, Henley JR, Cook T, McNiven MA (January 1997). "The dynamins: redundant or distinct functions for an expanding family of related GTPases?". Proceedings of the National Academy of Sciences of the United States of America. 94 (2): 377–384. Bibcode:1997PNAS...94..377U. doi:10.1073/pnas.94.2.377. PMC 34135. PMID 9012790.
  4. ^ Thoms S, Erdmann R (October 2005). "Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation". The FEBS Journal. 272 (20): 5169–5181. doi:10.1111/j.1742-4658.2005.04939.x. PMID 16218949.
  5. ^ Hinshaw JE, Schmid SL (March 1995). "Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding". Nature. 374 (6518): 190–192. Bibcode:1995Natur.374..190H. doi:10.1038/374190a0. PMID 7877694. S2CID 4365628.
  6. ^ a b c Praefcke GJ, McMahon HT (February 2004). "The dynamin superfamily: universal membrane tubulation and fission molecules?". Nature Reviews. Molecular Cell Biology. 5 (2): 133–147. doi:10.1038/nrm1313. PMID 15040446. S2CID 6305282.
  7. ^ Sundborger AC, Fang S, Heymann JA, Ray P, Chappie JS, Hinshaw JE (August 2014). "A dynamin mutant defines a superconstricted prefission state". Cell Reports. 8 (3): 734–742. doi:10.1016/j.celrep.2014.06.054. PMC 4142656. PMID 25088425.
  8. ^ a b Kong L, Sochacki KA, Wang H, Fang S, Canagarajah B, Kehr AD, et al. (August 2018). "Cryo-EM of the dynamin polymer assembled on lipid membrane". Nature. 560 (7717): 258–262. Bibcode:2018Natur.560..258K. doi:10.1038/s41586-018-0378-6. PMC 6121775. PMID 30069048.
  9. ^ Mattila JP, Shnyrova AV, Sundborger AC, Hortelano ER, Fuhrmans M, Neumann S, et al. (August 2015). "A hemi-fission intermediate links two mechanistically distinct stages of membrane fission". Nature. 524 (7563): 109–113. Bibcode:2015Natur.524..109M. doi:10.1038/nature14509. PMC 4529379. PMID 26123023.
  10. ^ Roux A, Uyhazi K, Frost A, De Camilli P (May 2006). "GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission". Nature. 441 (7092): 528–531. Bibcode:2006Natur.441..528R. doi:10.1038/nature04718. PMID 16648839. S2CID 4413887.
  11. ^ Macia E, Ehrlich M, Massol R, Boucrot E, Brunner C, Kirchhausen T (June 2006). "Dynasore, a cell-permeable inhibitor of dynamin". Developmental Cell. 10 (6): 839–850. doi:10.1016/j.devcel.2006.04.002. PMID 16740485.
  12. ^ Eschenburg S, Reubold TF (November 2018). "Modulation of dynamin function by small molecules". Biological Chemistry. 399 (12): 1421–1432. doi:10.1515/hsz-2018-0257. PMID 30067507. S2CID 51895475.
  13. ^ Camarero N, Trapero A, Pérez-Jiménez A, Macia E, Gomila-Juaneda A, Martín-Quirós A, et al. (September 2020). "Correction: Photoswitchable dynasore analogs to control endocytosis with light". Chemical Science. 11 (35): 9712. doi:10.1039/D0SC90189J. PMC 7495901. PMID 33016959.
  14. ^ Züchner S, Noureddine M, Kennerson M, Verhoeven K, Claeys K, De Jonghe P, et al. (March 2005). "Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease". Nature Genetics. 37 (3): 289–294. doi:10.1038/ng1514. PMID 15731758. S2CID 19191581.
  15. ^ Dhindsa RS, Bradrick SS, Yao X, Heinzen EL, Petrovski S, Krueger BJ, et al. (June 2015). "Epileptic encephalopathy-causing mutations in DNM1 impair synaptic vesicle endocytosis". Neurology. Genetics. 1 (1): e4. doi:10.1212/01.NXG.0000464295.65736.da. PMC 4821085. PMID 27066543.
[edit]
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