We are analyzing https://link.springer.com/article/10.1186/s12915-017-0474-3.

Title:
Hsp70 at the membrane: driving protein translocation | BMC Biology
Description:
Efficient movement of proteins across membranes is required for cell health. The translocation process is particularly challenging when the channel in the membrane through which proteins must pass is narrow—such as those in the membranes of the endoplasmic reticulum and mitochondria. Hsp70 molecular chaperones play roles on both sides of these membranes, ensuring efficient translocation of proteins synthesized on cytosolic ribosomes into the interior of these organelles. The “import motor” in the mitochondrial matrix, which is essential for driving the movement of proteins across the mitochondrial inner membrane, is arguably the most complex Hsp70-based system in the cell.
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Keywords {🔍}

pubmed, tim, hsp, article, protein, google, scholar, membrane, cas, mitochondrial, proteins, translocation, binding, central, pam, import, biol, motor, matrix, translocon, cell, complex, interaction, tom, hsps, domain, targeting, presequence, fig, sec, function, cytosolic, craig, channel, mitochondria, role, polypeptide, substrate, interactions, mol, ssb, site, membranes, model, called, jprotein, molecular, atp, ntd, chaperones,

Topics {✒️}

van der laan n-terminal α-helices protruding n-terminal ims-localized domain article download pdf tail-anchored protein integration yidc/oxa1/alb3 machinery c-terminal eevd tetrapeptide full size image proximity-specific ribosome profiling domain-related cochaperone tim16 n-terminal targeting sequences j-protein heterodimer pam18/pam16 adp/atp carrier cooperate carboxy-terminal segment play clathrin-coat disassembly illuminates power stroke model site-specific crosslinking experiments n-terminal targeting presequence facilitates lateral transfer tim44 c-terminal domain drives post-translational import abundant j-protein partner complex hsp70-based system annu rev biochem efficiently translocated post-translationally highly conserved j-domain lumenal j-domain functions genome biol evol peripheral membrane protein hsc70/hsp70 type performs d'silva dnaj-related protein drive directional movement biological processes—initial interaction privacy choices/manage cookies c-terminal eevd cleavable targeting sequence c-terminal domain hegde rs chirico wj frazier ae stop-transfer nat struct biol hsp90 molecular chaperones molecular chaperones hsp90 direct chaperone–receptor interactions approximately equal size large size compared glick bs membranes search search

Questions {❓}

Can Hsp70 proteins act as force-generating motors?
Does an individual nascent chain bind both Ssb and SRP?
Embracing the void--how much do we really know about targeting and translocation to the endoplasmic reticulum?
For example, do Hsp70s play a role in the recently identified SND targeting system to the ER that uses the SEC61 translocon [92]?
For many years two challenging questions have vexed workers studying PAM: what mechanistic principle(s) are behind motor function, and what motor characteristics drive motor efficiency?
How do J-proteins get Hsp70 to do so many different things?
How do polypeptides cross the mitochondrial membranes?
How does an import motor mechanistically drive efficient protein translocation?

Schema {🗺️}

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      headline:Hsp70 at the membrane: driving protein translocation
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         Hsp90 Binding Site
         Presequence
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