Innexin

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Innexin
Identifiers
SymbolInnexin
PfamPF00876
InterProIPR000990
TCDB1.A.25
OPM superfamily194
OPM protein5h1r

Innexins are transmembrane proteins that form gap junctions in invertebrates. Gap junctions are composed of membrane proteins that form a channel permeable to ions and small molecules connecting the cytoplasm of adjacent cells. Although gap junctions provide similar functions in all multicellular organisms, it was not known what proteins invertebrates used for this purpose until the late 1990s. While the connexin family of gap junction proteins was well-characterized in vertebrates, no homologues were found in non-chordates.

Innexins or related proteins are widespread among Eumetazoa, with the exception of echinoderms.[1]

Discovery[]

Gap junction proteins with no sequence homology to connexins were initially identified in fruit flies. It was suggested that these proteins are specific invertebrate gap junctions, and they were thus named "innexins" (invertebrate analog of connexins).[2] They were later identified in diverse invertebrates. Invertebrate genomes may contain more than a dozen innexin genes. Once the human genome was sequenced, innexin homologues were identified in humans and then in other vertebrates, indicating their ubiquitous distribution in the animal kingdom. These homologues were called "pannexins" (from the Greek pan - all, throughout, and Latin nexus - connection, bond).[3][4] However, increasing evidence suggests that pannexins do not form gap junctions unless overexpressed in tissue and thus, differ functionally from innexins.[5]

Structure[]

Innexins have four transmembrane segments (TMSs) and, like the vertebrate connexin gap junction protein, innexin subunits together form a channel (an "innexon") in the plasma membrane of the cell.[6] Two innexons in apposed plasma membranes can form a gap junction. Innexons are made from eight subunits, instead of the six subunits of connexons.[7] Structurally, innexins and connexins are very similar, consisting of 4 transmembrane domains, 2 extracellular and 1 intracellular loop, along with intracellular N- and C-terminal tails. Despite this shared topology, the protein families do not share enough sequence similarity to confidently infer common ancestry.

Pannexins are similar to innexins and are usually considered a sub-group, but they do not participate in the formation of gap junctions and the channels have seven subunits.[8][9]

Vinnexins, viral homologues of innexins, were identified in polydnaviruses that occur in obligate symbiotic associations with parasitoid wasps. It was suggested that vinnexins may function to alter gap junction proteins in infected host cells, possibly modifying cell-cell communication during encapsulation responses in parasitized insects.[10][11][12]

Function[]

Innexins form gap junctions found in invertebrates. They also form non-junctional membrane channels with properties similar to those of pannexons.[13] N-terminal- elongated innexins can act as a plug to manipulate hemichannel closure and provide a mechanism connecting the effect of hemichannel closure directly to apoptotic signal transduction from the intracellular to the extracellular compartment.[14]

The vertebrate homolog pannexin do not form gap junctions. They only form the hemichannel "pannexons". These hemichannels can be present in plasma, ER and Golgi membranes. They transport Ca2+, ATP, inositol triphosphate and other small molecules and can form hemichannels with greater ease than connexin subunits.[15]

Transport reaction[]

The transport reactions catalyzed by innexin gap junctions is:

Small molecules (cell 1 cytoplasm) ⇌ small molecules (cell 2 cytoplasm)

Or for hemichannels:

Small molecules (cell cytoplasm) ⇌ small molecules (out)

Examples[]

  • Caenorhabditis elegans
    • unc-7
    • unc-9
    • inx-3
  • Drosophila melanogaster
    • Inx2
    • Inx3
    • Inx4 (zero population growth, zpg)
    • Ogre
    • shaking-B
  • Hirudo medicinalis
    • Hm-inx1
    • Hm-inx2
    • Hm-inx3
    • Hm-inx6

See also[]

References[]

  1. ^ Hasegawa DK, Turnbull MW (April 2014). "Recent findings in evolution and function of insect innexins". FEBS Letters. 588 (8): 1403–10. doi:10.1016/j.febslet.2014.03.006. PMID 24631533. S2CID 25970503.
  2. ^ Phelan P, Stebbings LA, Baines RA, Bacon JP, Davies JA, Ford C (January 1998). "Drosophila Shaking-B protein forms gap junctions in paired Xenopus oocytes". Nature. 391 (6663): 181–4. Bibcode:1998Natur.391..181P. doi:10.1038/34426. PMID 9428764. S2CID 205003383.
  3. ^ Panchin Y, Kelmanson I, Matz M, Lukyanov K, Usman N, Lukyanov S (June 2000). "A ubiquitous family of putative gap junction molecules". Current Biology. 10 (13): R473-4. doi:10.1016/S0960-9822(00)00576-5. PMID 10898987. S2CID 20001454.
  4. ^ Kelmanson IV, Shagin DA, Usman N, Matz MV, Lukyanov SA, Panchin YV (December 2002). "Altering electrical connections in the nervous system of the pteropod mollusc Clione limacina by neuronal injections of gap junction mRNA". The European Journal of Neuroscience. 16 (12): 2475–6. doi:10.1046/j.1460-9568.2002.02423.x. PMID 12492443. S2CID 41324492.
  5. ^ Dahl G. & Harris A. 2009. Pannexins or Connexins? Chapter 12. In: A. Harris, D. Locke (eds.), Connexins: A Guide doi:10.1007/978-1-59745-489-6_12
  6. ^ Bao L, Samuels S, Locovei S, Macagno ER, Muller KJ, Dahl G (December 2007). "Innexins form two types of channels". FEBS Letters. 581 (29): 5703–8. doi:10.1016/j.febslet.2007.11.030. PMC 2489203. PMID 18035059.
  7. ^ Oshima A, Matsuzawa T, Murata K, Tani K, Fujiyoshi Y (March 2016). "Hexadecameric structure of an invertebrate gap junction channel". Journal of Molecular Biology. 428 (6): 1227–1236. doi:10.1016/j.jmb.2016.02.011. PMID 26883891.
  8. ^ Michalski K, Syrjanen JL, Henze E, Kumpf J, Furukawa H, Kawate T (February 2020). "The cryo-EM structure of a pannexin 1 reveals unique motifs for ion selection and inhibition". eLife. 9: e54670. doi:10.7554/eLife.54670. PMC 7108861. PMID 32048993.
  9. ^ Qu R, Dong L, Zhang J, Yu X, Wang L, Zhu S (March 2020). "Cryo-EM structure of human heptameric Pannexin 1 channel". Cell Research. 30 (5): 446–448. doi:10.1038/s41422-020-0298-5. PMC 7196123. PMID 32203128.
  10. ^ Turnbull M, Webb B (2002). Perspectives on polydnavirus origins and evolution. Advances in Virus Research. Vol. 58. pp. 203–54. doi:10.1016/S0065-3527(02)58006-4. ISBN 9780120398584. PMID 12205780.
  11. ^ Kroemer JA, Webb BA (2004). "Polydnavirus genes and genomes: emerging gene families and new insights into polydnavirus replication". Annual Review of Entomology. 49 (1): 431–56. doi:10.1146/annurev.ento.49.072103.120132. PMID 14651471.
  12. ^ Marziano N.K.; Hasegawa D.K.; Phelan P.; Turnbull M.W. (October 2011). "Functional Interactions between Polydnavirus and Host Cellular Innexins". Journal of Virology. 85 (19): 10222–9. doi:10.1128/jvi.00691-11. PMC 3196458. PMID 21813607.
  13. ^ Bao L, Samuels S, Locovei S, Macagno ER, Muller KJ, Dahl G (December 2007). "Innexins form two types of channels". FEBS Letters. 581 (29): 5703–8. doi:10.1016/j.febslet.2007.11.030. PMC 2489203. PMID 18035059.
  14. ^ Chen YB, Xiao W, Li M, Zhang Y, Yang Y, Hu JS, Luo KJ (May 2016). "N-TERMINALLY ELONGATED SpliInx2 AND SpliInx3 REDUCE BACULOVIRUS-TRIGGERED APOPTOSIS VIA HEMICHANNEL CLOSURE". Archives of Insect Biochemistry and Physiology. 92 (1): 24–37. doi:10.1002/arch.21328. PMID 27030553.
  15. ^ Shestopalov VI, Panchin Y (February 2008). "Pannexins and gap junction protein diversity". Cellular and Molecular Life Sciences. 65 (3): 376–94. doi:10.1007/s00018-007-7200-1. PMID 17982731. S2CID 23181471.

Further reading[]

External links[]

This article incorporates text from the public domain Pfam and InterPro: IPR000990

As of , this article uses content from "1.A.25 The Gap Junction-forming Innexin (Innexin) Family", which is licensed in a way that permits reuse under the Creative Commons Attribution-ShareAlike 3.0 Unported License, but not under the GFDL. All relevant terms must be followed.

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