The mammalian pannexin family is homologous to the invertebrate innexin gap junction proteins

Baranova, Ancha; Ivanov, Dmitry; Petrash, Nadezda; Pestova, A A; Skoblov, Mikhail; Kelmanson, Ilya V.; Shagin, Dmitry A.; Nazarenko, Svetlana; Geraymovych, Elena; Litvin, Oxana; Tiunova, Anya; Born, Timothy L.; Usman, Natalia; Staroverov, Dmitry B; Lukyanov, Sergey; Panchin, Yu. V.

doi:10.1016/j.ygeno.2003.09.025

Cited by 435 publications

(495 citation statements)

References 26 publications

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“…Recently, a homolog of innexins was found in vertebrate animals, and named pannexins (Baranova et al, 2004). Pannexins are thought to be tetra membrane-spinning proteins and are known to form functional channels from expression studies in Xenopus oocytes (Bruzzone et al, 2003), but whether pannexins form functional channels in vertebrate animals or are vestige proteins replaced by connexins is still unknown.…”

Section: Discussionmentioning

confidence: 99%

Immunocytochemical study of gap junction-related protein, innexin 2, in Periplaneta americana (Blattodea: Blattidae)

Fushiki

Yoshimura

Endo

2010

Appl. Entomol. Zool.

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Gap junctions are intercellular junction apparatus found in almost all multicellular animals and are involved in direct intercellular communication. Those of invertebrate animals consist of the innexin protein family. We developed antibodies against peptide fragments of Bombyx mori innexin 2, and examined tissues of Periplaneta americana by Western blotting, immunohistochemistry and immunoelectron microscopy. Intense immunoreactivity of innexin 2 was found in the midleg, gizzard and thoracic muscular tissues. Immunoelectron microscopy showed that immunogold particles of innexin 2 were aggregated around cell adhesion structures between muscle fibers. These results suggest that innexin 2 is expressed in the muscle cells of cockroaches and is involved in synchronization of muscle contraction.

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Section: Discussionmentioning

confidence: 99%

Immunocytochemical study of gap junction-related protein, innexin 2, in Periplaneta americana (Blattodea: Blattidae)

Fushiki

Yoshimura

Endo

2010

Appl. Entomol. Zool.

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“…In addition to their role in nucleotide release from apoptotic cells, the pannexin channels are also involved in regulating the integrity of the dying cells, 63 regulation of vascular constriction via nucleotides released by non-apoptotic mechanisms, 64 and cancer cell migration. 65 Owing to the ubiquitous expression 66 and vast regulatory mechanisms of Panx1 activation, 61,67 novel cell-type-specific knock-out and transgenic mice affecting apoptosis-specific activation may be necessary to understand its involvement during cell clearance in vivo. Numerous knock-out studies have been performed on other proteins involved in different aspects of these attraction signals.…”

Section: Steps Involved In Clearancementioning

confidence: 99%

Do not let death do us part: ‘find-me’ signals in communication between dying cells and the phagocytes

2016

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The turnover and clearance of cells is an essential process that is part of many physiological and pathological processes. Improper or deficient clearance of apoptotic cells can lead to excessive inflammation and autoimmune disease. The steps involved in cell clearance include: migration of the phagocyte toward the proximity of the dying cells, specific recognition and internalization of the dying cell, and degradation of the corpse. The ability of phagocytes to recognize and react to dying cells to perform efficient and immunologically silent engulfment has been well-characterized in vitro and in vivo. However, how apoptotic cells themselves initiate the corpse removal and also influence the cells within the neighboring environment during clearance was less understood. Recent exciting observations suggest that apoptotic cells can attract phagocytes through the regulated release of 'find-me' signals. More recent studies also suggest that these find-me signals can have additional roles outside of phagocyte attraction to help orchestrate engulfment. This review will discuss our current understanding of the different find-me signals released by apoptotic cells, how they may be relevant in vivo, and their additional roles in facilitating engulfment.

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Section: Pannexin Genesmentioning

confidence: 61%

“…23 A similar pattern is true for the murine pannexin genes, where Panx1 and Panx3 genes are located on chromosome 9, whereas Panx2 is found on chromosome 15. 23 It is interesting to note that Panx1 and Panx3 in both species also share a higher degree of sequence homology with each other (59-62% conserved) than with Panx2 (48-56% conserved). 9 Unlike the connexin family of gap junction proteins, pannexins have a complex gene structure (Figure 2), including several exons and introns covering from ∼6 kb (Panx2 and Panx3) to up to 40 kb of genomic sequence (Panx1) in both mouse and human genomes.…”

Section: Pannexin Genesmentioning

confidence: 61%

“…9 Unlike the connexin family of gap junction proteins, pannexins have a complex gene structure (Figure 2), including several exons and introns covering from ∼6 kb (Panx2 and Panx3) to up to 40 kb of genomic sequence (Panx1) in both mouse and human genomes. 23 Human and mouse Panx1 are encoded within five exons with four introns. Human PANX2 has four coding exons, whereas mouse Panx2 appears to have just three exons.…”

Section: Pannexin Genesmentioning

confidence: 99%

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The cellular life of pannexins

Peñuela

Laird

2012

WIREs Membr Transp Signal

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The mammalian pannexin family of channel-forming proteins consisting of Panx1, Panx2, and Panx3 has received considerable attention in the last 10 years given their newly discovered physiological roles in development and disease. Pannexins exhibit diverse subcellular profiles indicating that they may serve distinct roles in cells and tissues of different origin. This complexity in cellular residencies may be rooted in the fact that pannexin genes consist of multiple exons that have led to the identification of several splice variants. Additionally, post-translational modifications, especially N-glycosylation, appear to be important in regulating trafficking and intermixing of pannexin family members increasing the diversity of assembled channels. These long-lived membrane proteins are typically trafficked through the classical secretory pathway before reaching the plasma membrane although Panx2 tends to often be retained in intracellular compartments. Trafficking, stability, and function of pannexins likely enlist the services of an interactome that continues to expand. The research field has been amazed by the fact that Panx1 null mice are generally healthy with distinct phenotypes only being revealed when mutant mice encounter additional stress or have comorbidities. The emerging field of pannexin biology has also begun to explore the relationships and potential cross-talk between pannexin channels and connexin hemichannels. It is imperative to dissect the different constituents of the channels and the molecules that pass through these distinct channel types. Finally, as witnessed in connexin biology throughout the 90s, the field awaits to see if germline mutations in the genes that encode pannexins also cause disease.

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The mammalian pannexin family is homologous to the invertebrate innexin gap junction proteins

Cited by 435 publications

References 26 publications

Immunocytochemical study of gap junction-related protein, innexin 2, in Periplaneta americana (Blattodea: Blattidae)

Immunocytochemical study of gap junction-related protein, innexin 2, in Periplaneta americana (Blattodea: Blattidae)

Do not let death do us part: ‘find-me’ signals in communication between dying cells and the phagocytes

The cellular life of pannexins

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